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					                             Camel and Biomolecular Sciences
                             University of Tehran, Tehran, Iran
                                     22 December 2010
                                    Camel: an important species

                                           A. Niasari-Naslaji*

    Dept. Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran

FAO (2008) announced that there are 24,664,228 heads of camel in the world from which only
152,000 heads belongs to Iran (0.6%). According to the same source,the majority of camel
population belongs to African countries (20,959,015; 85%); while only 822,570 (3%) belongs to the
countries around Persian Gulf and Oman sea. Nevertheless, based on documented records in Web of
Science (06/12/2010), the first line of camel research does not belong to any of these countries but
is dedicated to USA with 494 articles (14.2%). Islamic Republic of Iran stands for the 7th rank in
camel research in the world with production of 184 articles (5.3%). The delicate question is “why
the western countries without local access to camel have an interest on camel research?” In other
words, “what are the peculiarities in camel species that tease the appetites for research in this
unique species?” According to the narration by the Prophet of Islam (PUH), “Camel brings
superiority for its owner”. Therefore, since long time ago camel was recognized as a valuable
animal with therapeutic products such as milk, urine, hump and meat. Recent research reveals
interesting characteristics in camel milk and immunoglobulin. Lack of light chain, cell permeability,
ability to cross blood brain barrier, higher specificity with none to extremely low cross-reactivity,
higher thermal stability (functional at 90 °C), higher pH range tolerance (pH 2-10) and higher water
solubility without any aggregation are the main and unique characteristics of camel
immunoglobulin. These peculiarities grab the attention of researchers to use camel immunoglobulin
for therapeutic and diagnostic purposes. In summary, research in camel milk and immunoglobulin
has to become the priority in research in the countries that have local access to this precious species.
Extensive research on extracting and mass producing the biological products from camel milk and
immunoglobulin may open a new horizon in preventing, threating and diagnosing human diseases
andenhance the national gross income of the camel holding countries.

Keywords: Camel; population; immunoglobulin, milk



*
 Corresponding author: Address; P.O.Box: 14155-6453, Tehran, Iran; Tel: +9821 6111
7136; Fax: +9821 6693 3222; Email: niasari@ut.ac.ir; Website: www.cevetut.com,
Center of Excellence for Veterinary Research on Iranian Indigenous Animals
(Prof. Amir Niasari-Naslaji)

                                                   1
                               Camel and Biomolecular Sciences
                               University of Tehran, Tehran, Iran
                                       22 December 2010
Comparative analysis of the heme binding pockets of three homologoushemoglobins:
                                  Camel hemoglobin specification

  F. Rezaei1, M. Sharifahmadian1, A. Madadkar2, A.A. Moosavi-Movahedi2, M. Habibi-
                                                       *
                                               Rezaei1

           1
               School of Biology, College of Science, University of Tehran, Tehran, Iran,

       2
           Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

In this study, comparison have been made among three homologoushemoglobins; human
(HHb), bovine (BHb) and camel (CHb), for their representative susceptibility to oxidation.
The order of their susceptibilities was observed to be as CHb>HHb>BHb. Hemoglobin of
camel is more prone to be oxidized than the next two homologues. Since three dimensional
structure of the CHb has not yet resolved, using molecular simulation approach the
structure of the CHb was simulated            and resulted coordinations were verified. Then,
looking for the source of observed differences on heme to hemine conversion, docking
analysis were directed to heme binding pockets and LIG-plots were constructed for the
three heme binding pockets. Interestingly, more hydrophobic environment was resulted for
heme pocket in CHb than the next two molecules and pocket hydrophobicity seems to be
well correlated with oxidation susceptibility.




* Corresponding author: Dr Mehran Habibi-Rezaei, mhabibi@khayam.ut.ac.ir

                                                   2
                                        Camel and Biomolecular Sciences
                                        University of Tehran, Tehran, Iran
                                                22 December 2010


    Antiserum production in immunized camel by the venom of Hemiscorpiuslepturus
                                   scorpion: evaluation of neutralizing test in vivo

        M. Behdani1, M. Hosseininejad Chafi2, S. Zeinali1, M. Karimipour1, H. Khanahmad
Shahreza3, P. Ghasemi2,4, N. Asadzadeh5, A. Ghamnak2, K. Pooshang Bagheri2, H. Ahari6,
                                                  D. Shahbazzadeh2*
                           1
                               Department of Molecular Medicine, Pasteur Institute of Iran
                      2
                          Medical Biotechnology Research Center, Pasteur Institute of Iran
            3
                Department of BCG, Research-Production Branch, Pasteur Institute of Iran
4
 Biotechnology Research Center, Shahrekord Branch of Islamic Azad University, Shahrekord, Iran
                  5
                      Department of Breeding, Animal Sciences Research Institute of Iran
    6
        Food Hygiene, Science and Research Branch of Islamic Azad University Tehran, Iran


Scorpion envenomation is considered as one of the Public Health problems in some
countries in the world including Iran. Annually, approximately 30,000 scorpion stings
happen in Iran from which 12% belongs to Hemiscorpiuslepturus (special small closely
spaced, bead-shaped jointed tail, similar in the shape to a cows tail, and is locally called
„„gaodim‟‟ (Gao, cow; dim, tail)) with 95% mortality. The main treatment is antiserum
therapy which is produced in horse and is the only way to neutralize the venom. Due to the
anaphylactic shock of the horse antiserum in some of the stung patients other source of
antiserum is recommended. In this study the ability of produced camel antiserum in
neutralizing the scorpion venom of Hemiscorpiuslepturus was performed in Balb/c model.
Camel is an animal model that genetically is compatible with human genome utilized in this
research to produce antiserum against scorpion venom. Two camels were used for
immunization with the venom of Hemiscorpiuslepturus. ELISA method was used to
confirm the immunity. Antiserum was produced and used for neutralizing test. The
precipitated antiserum with saturated ammonium sulfate (SAS) was also used to perform
the neutralizing test in mice.The results indicated that the amount of 200 µl of antiserum
and 400 µl of SAS antiserum were able to neutralize the amount of 1 LD100 of the venom
and the survived the mice from death. The result indicated that camel antiserum against
scorpion venom is capable to neutralize the crude venom in mice model. Due to the safety
of camel serum in human, it is suggested that the produced antiserum in camel can be
substitute with the traditional horse antiserum in scorpion stung patients.
Keywords: Antiserum, camel, scorpion venom, Hemiscorpiuslepturus



*Corresponding author: Dr. Delavar Shahbazzadeh, shahbazzadeh@yahoo.com
                                                           3
                                  Camel and Biomolecular Sciences
                                  University of Tehran, Tehran, Iran
                                          22 December 2010
              Functional properties of bioactive peptides produced from camel milk
                     M. Salami 1*, F. Moosavi-Movahedi1, M.R. Ehsani2, R. Yousefi3,

                             A. Niasari-Naslaji4 and A.A. Moosavi-Movahedi1

               1
                   Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

  2
      Department of Food Science and Engineering, Faculty of Bio-system Engineering, College of
                      Agriculture and Natural Resources, University of Tehran, Karaj, Iran

          3
           Department of Biology, College of Sciences, Shiraz University, 71454, Shiraz, Iran

      4
       Dept .Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran

Milk proteins exert a wide range of nutritional, functional and biological activities.
Bioactive peptides encrypted in milk proteins are a major source for novel functional food
ingredients. These peptides can be produced in vivo during gastrointestinal digestion or in
vitro throughout food processing using specific enzymes. Milk protein derived peptides
have different functionality including antioxidant activity, antimicrobial activity and blood
pressure–lowering effect. Most of these foods are produced using bovine‟s milk proteins
but bovine milk allergy by far is the most prevalent food allergy especially in children and
β-lactoglobulin (β-LG) is considered the dominant bovine milk allergen. Camel whey lacks
β-LG and similar to human milk α-Lactalbumin is its predominant whey protein. It is well
known that the oxidative stress due to free-radicals is considered to be responsible for many
chronic diseases such as cardiovascular diseases, diabetes, cataracts, neurodegenerative
disorders, and certain types of cancer and aging. The result of our studies showed that the
bioactive peptides derived from camel milk protein had higher functionality including
antioxidant activity, anti-hypertension effect and antimicrobial activity comparing to
bioactive peptides from bovine milk proteins. Considering the health effect of camel milk
proteins and its bioactive peptides, it could be the 'super food' of the future.

Keywords: camel milk, bioactive peptides, functional food

*Corresponding Author: msalami@ut.ac.ir


                                                        4
                             Camel and Biomolecular Sciences
                             University of Tehran, Tehran, Iran
                                     22 December 2010
       Bioactive Peptides derived from camel whey proteins promote osteogenic
                        differentiation of unrestricted somatic stem cell
         I. Khaki Najafabadi1,2*, B. Zeynali1 , M. Salami2, F. Moosavi-Movahedi2,

                     M. Mowlavi Vardanjani 1 and A.A. Moosavi-Movahedi2

  1
   Developmental Biology lab, School of Biology, College of Science, University of Tehran, Iran

          2
              Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

In recent years, strong efforts have been made to develop stem cell based therapies for bone
and cartilage regeneration. Unrestricted somatic stem cells (USSC) show strong
differentiation capacity into osteogenic and chondrogenic lineage. Based on in vitro and in
vivo studies, it has been recently reported that milk whey protein, especially its basic
protein fraction, contains several components capable of both promoting bone formation
and inhibiting bone resorption. Whey proteins are a major source of bioactive peptides. In
this study,the effects of bioactive peptide of whey protein was investigated on USSCs
during their osteogenicdifferentiation.To address this question, USSCs were isolated from
mononuclear cells of the umblinical cord. USSCs were then cultured in the presence of
osteogenic medium with or without the bioactive peptides isolated from whey protein using
digestive enzymes. The expression of specific osteogenic genes and the level of
mineralization were examined in USSCs cultured for 21 days. RT-PCR analysis indicated
that the mRNA expression level of osteocalcin (OC) and Runx2 (osteogenic regulator) were
up-regulated by bioactive peptides. Moreover, our results revealed that production of bone
matrix was significantly increased by these bioactive peptides. All together, our results
indicate that the peptide fraction obtained from camel whey could promote osteogenesis,
introducing these peptides as a nutraceuticals and natural drugs useful for bone
regeneration.
Keywords: USSCs, Osteogenic differentiation, bone regeneration, bioactive peptide



* Corresponding author: Tel: 61112629 ; Fax: 66492992              ; Email:
bzeynali@khayam.ut.ac.ir

                                                   5
                          Camel and Biomolecular Sciences
                          University of Tehran, Tehran, Iran
                                  22 December 2010
     Antibacterial activity of the lactoperoxidase system in camel milk against

                       Gram-positive and Gram-negative bacteria

                                              *
             M. Bolorimoghadam1, S. Zibaei2 , M. Saleh1, H. Norozi Moghadam2
                           1
                               Pyamenor University, Mashhad, Iran

       2
           Razi Vaccine and Serum Research Ins., North-East Branch, Mashhad, Iran

Lactoperoxidase (LPO) is an oxidative enzyme that is found in milk of mammals including
camel. Lactoperoxidase for bacteriostatic activity to thiocyanate and hydrogen peroxide
needs. Lactoperoxidase enzyme was extracted and purified with centrifuge, ion exchange
C-50 chromatography and sephdex G-100 gel filtration from raw milk. The activity of
enzyme was measured by using Tetra methylbenzidine and assay of enzyme was carried
out by Bradford method. To evaluate the purity of the enzyme Polyacrylamide gel
electrophoresis     was    used.     Staphylococcus    aurous   (Gram-positive     bacteria)
andPseudomonasaeruginosa (Gram-negative bacteria) obtained from Razi vaccine and
serum research institute. We were found number of bacteria by colony count and used 10-6
dilution per ml for accomplishment of tests. We made 4 test groups (for each bacteria) and
one control group that there were four replications with equal conditions. Test groups
include 2 reagent groups (H2O2, tiocyanate) and one groupcontainingH2O2 and tiocyanate
together and one complete system {H2O2 (0.03Mm), tiocyanate (1Mm), LPO
(0.02µg/ml)}. The number of bacteria calculated at 0, 60 and 360 mints with colony-count
method on Blood agar. Based on the test ratios (Chi-square), significantly (P = 0.0001)
between the effects of complete system (with a 70 percent reduction in minute 360 for
Staphylococcus aurous and (with a 63 percent reduction in minute 360 for Pseudomonas
aeruginosa) with participants of other materials in response was seen to antibacterial
activity. As a result, Lactoperoxidas enzyme was extracted from Camel Milk has a
significant anti-bacterial activity on Gram-positive and gram-negative bacteria.

Keywords: Camel milk; lactoperoxidase; Staph. aureus; Pseudomonas aeruginosa


*
Corresponding author: Dr Saeed Zibaee, Tel: 0511 8405888; Email: s.zibaei@rvsri.ir
                                                  6
                         Camel and Biomolecular Sciences
                         University of Tehran, Tehran, Iran
                                 22 December 2010



                          Cancer therapy with camel antibody

                M. Behdani*, S. Zeinali, M. Karimipour, D. Shahbazzadeh
          Molecular Medicine Department, Pasteur Institute of Iran, Tehran, Iran
In molecular approach, serum of camel contains a unique type of antibodies devoid of light
chains. Since the light chain is missing, the heavy-chain antibodies should bind their
antigen by one single domain, the variable domain of the heavy immunoglobulin chain.
This type of camel antibody has unique character like harsh medium resistant and ease of
expression and purification in the bacterial system. Recombinant monoclonal antibodies
(mAbs) are one of the most prolific drug classes in oncology and hematology with many
molecules under clinical development or usage. They were initially derived from murine
mAbs based on hybridoma technology. Several of these antibodies are based on mouse
antibody. Camel antibodies can be replaced with these therapeutic antibodies because of
close homology to human VH fragments. Our group focuses on development of camel
antibody against Vascular Endothelial Growth Factor Receptor-2 (VEGFR-2) which
overexpressed in many types of tumors. VEGFR-2 is one of the important factors in tumor
angiogenesis and a factor of choose for tumor therapy.

Keywords: Single chain antibody, cancer, camel




*Corresponding author: Dr Mahdi Behdani, Tel: 021-66480780;
Email: Behdani73042@yahoo.com

                                             7
                           Camel and Biomolecular Sciences
                           University of Tehran, Tehran, Iran
                                   22 December 2010


                 Effect of camel milk on different cell lines and normal cells
                                 M. Ahmadi1, Mohsen Fathi Najafi2*
                             1
                                 Pyamenor University, Mashhad, Iran

        2
            Razi Vaccine and Serum Research Ins., North-East Branch, Mashhad, Iran

Milk is one of important food and immunogenic compound that any animal is produce for
its infant. Regarding to traditional medicine, camel milk has very important role for
treatment and feeding of different type of patients. In this study effect of camel milk on
different cell lines such as MCF-7, Vero, BHK21, McCoy and its comparison with normal
cells ( such as spleen, liver, kidney and lymphocyte) was investigated. Camel milk was
collected freshly and it was applied to the cell culture plates for different cells at various
incubation times (24, 48 and 72 hours). After time incubation, the cell morphology and its
viability were controlled under inverted microscope and MTT assay respectively. The same
experiment was performed for partial purified proteins of camel milk. The results of this
study were analyzed statistically by SPSS software and shown that camel milk could effect
on cell lines and reduce their viability and kill the cells. In contrast camel milk increased
half life of normal cell compare with controls during incubation time. With respect to these
results it could be suggested that camel milk has capability for more study for application in
medicinal use.
Keywords: Camel milk, cell lines, Apoptosis, MTT assay




*Corresponding author: Dr Mohsen Fathi Najafi, Tel: 0511 8405888; Email:
Najafi99@yahoo.com


                                                 8
                                 Camel and Biomolecular Sciences
                                 University of Tehran, Tehran, Iran
                                         22 December 2010
       Camel αS1-Casein: Thermal and Chaperone Behaviors of Phosphorylated and
                                        Dephosphorylated States

            Badraghi J.1,2*, Moosavi-Movahedi A.A.2, Saboury A.A.2 ,Niasari-Naslaji A.3,

                                    Sharifizadeh A.1,2, and Banaei A.1,2

        1
            Applied Science Institute (ACECR), University of ShahidBeheshti, Tehran, Iran

            2
                Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

3
    Dept. Clinical Science, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran


Protein aggregation is the leading cause of more than 20 different of so called protein
conformational diseases such as Alzheimer‟s, Parkinson, Huntington‟s and cataract. The
aim of this study was the extraction, purification and dephosphorylation of camel αS1
casein in order to study the thermal behavior and chaperone activity of αS1 casein on the
anti aggregation of insulin and catalase. Camel αS1-CN was purified, using diethyl amino
ethyl (DEAE) cellulose as the anion exchanger matrix and the purity of the protein sample
was analyzed using SDS-PAGE and urea PAGE. Potato acid phosphates was used to
remove the phosphate groups of the casein and degree of dephosphoryalation was assessed
by using different techniques, including SDS-PAGE, Urea-PAGE and an spectroscopic
methods. . The thermal profile of the protein in phosphorylated and totally
dephosphorylated states was monitored by following the change of intrinsic fluorescence
intensity under forward- and backward temperatures between 10 to 90 ºC. On the base of
this thermal stability of phosphorylated camel αS1 caseins were higher than
dephosphoryated αS1-CN. Phosphorylated camel αS1 casein inhibits the aggregation of
insulin and catalase. Our results indicate that dephosphorylated camel αS1 caseins reduce
chaperone activity of casein but still show chaperone ability to some extent. The chaperone
ability of the caseins depend mainly on the hydrophobic parts of the protein. Decreasing of
the phosphate concentrations in the casein due to the dephosphorylation caused reduction in
repulsive electrostatic interactions between negative charged αS1-CN, and the net negative
charge of insulin molecules, resulting in the lower exposure of hydrophobic patches of
casein and its reduced chaperone ability. In contrast, at high phosphate concentrations
(phosphorylated casein), the higher repulsive electrostatic interactions between negative
charged αS1-CN, and the net negative charge of insulin molecules, resulting in the higher
exposure of hydrophobic patches of casein and its enhanced, chaperone ability.



* Corresponding author: Dr Badraghi, badraghi@ibb.ut.ac.ir


                                                     9
                             Camel and Biomolecular Sciences
                             University of Tehran, Tehran, Iran
                                     22 December 2010

       Binding of oleic acid to camel holo α-lactalbumin at high temperature and
                        its influence on the structure and stability


M.S. Atri1*, A.A. Saboury1, A.A. Moosavi-Movahedi1, B. Goliaei1 and A. Niasari-Naslaji2
          1
              Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
   2
    Dept .Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran



The interaction of camel holo α-lactalbumin (α-La) with oleic acid at 60 °C was
investigated by fluorescence spectroscopy and circular dichroism (CD). A little change in
the secondary structure of the protein was observed upon ligand binding along with
enhanced tryptophan fluorescence emission. Fluorescence spectroscopy showed that camel
holo α-La has one binding site for oleic acid with association constant of 4.87×104 M-1.
This result shows that higher temperature enables the protein interaction with fatty acids
without calcium removal. Cytotoxic α-La –oleic acid and α-La –linoleic acid complexes
generated by adding fatty acid to camel holo α-La at 60 °C (referred to as La-OA-60 and
La-LA-60 state, respectively). Structural properties of these complexes were studied and
compared to the camle α-La. Also their stability toward thermal denaturation was
measured. Fatty acid bounded proteins appear to have lower stability than camle α-La.
Although the temperature at the transition midpoint is 5 °C lower for La-LA-60 and its
structure seems more disrupted, these two complexes have similar cytotoxic effect to
DU145 human prostate cancer cells.

Keywords: α-lactalbumin, fatty acid, fluorescence spectroscopy




*Correspondoing Author: Tel: +98-21-61113381 ; Fax: +98-21-66404680 ; Email:
atri@ibb.ut.ac.ir
                                                  11
                         Camel and Biomolecular Sciences
                         University of Tehran, Tehran, Iran
                                 22 December 2010


       Camel Beta-casein as a suitable vehicle for curcumin encapsulation and

                  solubilization: anticancer and antioxidant approach

    M. Esmaili*, S.M. Ghafari, Z. MoosaviMovahedi, M. Atri, A.A. Moosavi-Movahedi

       Institute of Biochemistry and Biophysics, University of Tehran, Tehran,Iran

Curcumin is a potent anticancer and antioxidant natural polyphenol poorly soluble in
aqueous solution. Beta-casein (B-CN), an amphiphilic self-assembling protein that can
form micellar nanostructures, which could be used as a vehicle for hydrophobic therapeutic
agents such as curcumin. In this study, camel B-CN was used for curcumin encapsulation.
Critical association concentration of camel B-CN was determined at 25, 30 and 37°C using
pyrene fluorescence and the solubility of curcumin was evaluated according to the solvent-
evaporation technique. Camel B-CN improved the solubility of curcumin at least 2500
folds. Analysis of fluorescence emission of curcumin showed that hydrophobic interactions
are predominant in its formulation with B-CN. Moreover, the cytotoxicity of curcumin to
human leukemia cell line K-562 was enhanced in the presence of B-CN micelles giving
inhibitory concentration (IC50) values of 26.5 and 17.7 µM for free and encapsulated
curcumin, respectively. Antioxidant activity of curcumin encapsulated in B-CN was higher
than that of both free B-CN and curcumin.

Keywords:Beta casein micelles, curcumin, solubility, encapsulation, fluorescence




*
Corresponding Author : mesmaili@ ibb.ut.ac.ir




                                            11
                          Camel and Biomolecular Sciences
                          University of Tehran, Tehran, Iran
                                  22 December 2010



  The role of temperature on self-association of beta-caseins from camel and bovine
                                            milk

                 A. Sharifizadeh*, A. A.Saboury and A. A.Moosavi-Movehedi

       Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

Beta-casein as a major group of milk proteins is a very amphipathic protein due to a large
hydrophobic domain in C-terminal and a highly charged N-terminal hydrophilic domain,
containing the phosphate center., Through its structure, beta-casein has a strong inherent
tendency to self-associate into micelles of 15 to 60 molecules and act as emulsifier same as
detergents. Association and conformational changes can have a major influence on the
function of beta-caseins. Therefore studies on this behavior are important.In this study,
biophysical techniques such as Differential Scanning Calorimetry (DSC), Circular
Dichroism(CD) and fluorescence spectroscopy were employed to investigate the
association and conformational changes of beta casein, One of the goals of this study was to
understand the relationship between primary and secondary structure of beta-casein and its
self-association behavior. For realizing such relations and differences of structure on self-
association, beta-casein from two different source of camel and bovine milk was used. Due
to the importance of thermal process in dairy industry, we focused on structure of beta-
casein upon the effect of temperature and compared at physiological temperature.The
results from fluorescence and CD spectra of the thermally stressed indicated that significant
differences in reversible protein conformation and show the association for protein due to
conformational changes. DSC supports the aforementioned evidences and indicated self-
association for beta-casein of camel and bovine milk at different Tm in reversible
phenomena. It can be concluded that camel beta-casein may have better functions due
stronger self-association properties.



*Corresponding author: Tel: (+9821) 61113381; Fax: (+9821) 66404680; sharifiz@ut.ac.ir


                                             12
                         Camel and Biomolecular Sciences
                         University of Tehran, Tehran, Iran
                                 22 December 2010



            Antioxidant effect of the mixture of camel beta casein and aloin

     F. Ghamari*, S. M. Ghafari, M. Salami, F. Farivar and A.A. Moosavi-Movahedi

       Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.

Nutrition is the key to good health. Studies have shown that regular consumption of natural
antioxidant is strongly associated with a reduced risk of developing chronic diseases such
as cancer and cardiovascular disease. In the last few years intensive research has been
conducted on the possibilities of designing new dietary foods containing high amount of
functional ingredient including natural antioxidant because different antioxidants serve
different purposes in the body. Aloe vera belongs to the Aloaceae family and actually is a
commercial and medicinal important. Many active components have been isolated from
Aloe species and studied for their biological activities. Among them, aloin and aloe-emodin
have been identified as the main active components. In this study the total antioxidant
capacity (TAC) of camel beta caseins and aloin were investigated using spectrophotometry
ABTS-based     method     (reduction   of   the   cation   radical   of      2,20-azinobis(3-
ethylenebenzothiazoline-6-sulfonic acid(ABTS)). Our results in this paper indicated that
both camel beta casein and aloin showed antioxidant activity when measured individually.
When the complex mixture of both camel beta casein and aloin were used higher
antioxidant activity was observed. The result of our study opens a new perspective into
producing dietary functional food using aloe vera and camel milk proteins.




*Corresponding author: f.ghamari@ibb.ut.ac.ir

                                            13
                             Camel and Biomolecular Sciences
                             University of Tehran, Tehran, Iran
                                     22 December 2010



  Comparison of the Polymerization Activity of Camel and Sheep Purified Tubulin

                    Y. Sefidbakht1*, A. Dadras1, A. Naghshineh1, Gh. Riazi1,
                          A. Niasari-Naslaji2, A. A. Moosavi-Movahedi1
          1
              Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
   2
    Dept. Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran



Microtubules are the most important proteins existing in eukaryotic cells specially neurons.
Functional roles of microtubules are significant for instance; in cell organization,
intracellular vesicle transport, cell division and cell signaling. Microtubules are hollow
cylindrical rods with external diameter of 25 nm and internal diameter of 17 nm. They‟re
composed of tubulin dimers which form protofilaments. Lateral contacts of protofilaments
(5 to 15) make a microtubule. Microtubule polymerization has three different phases
including nucleation, elongation and termination (or steady state) which require GTP
hydrolysis to perform. Each microtubule has minus and positive ends. On the basis of
Penrose and Hameroff hypothesis, the protein networks of microtubules are responsible for
intelligence manners of living organisms. In these theories, in fact microtubules supposed
as quantum computers of living organisms. Here, it was tried to find a relation between the
activity of this protein in sheep and camel and their intellectual behaviors. Increase in the
polymerization and length of microtubules is important for memory optimization. Thus we
can state that if organism‟s microtubules have better activity, it would be possible to be
more intelligent. From an animal behavior point of view, it seems that camel has better
memory than sheep. Hence,in order to compare polymerization potential of purified
tubulin, tubulin polymerization was studied by turbidimetry method in wavelength of 350
nm. Results show that activity of camel tubulin was well above (30%) of sheep tubulin.

Keywords: Camel, microtubule, intelligence


*Corresponding   author: Tel:              (+9821)     61113381;      Fax:   (+9821)     66404680;
Email:Y.Sefidbakht@ibb.ut.ac.ir

                                                  14

				
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