Isolation and characterization of serum albumin from Camelus dromedarius

Malik,Ajamaluddin; Al-Senaidy,Abdulrahman; Skrzypczak-Jankun,Ewa; Jankun,Jerzy

doi:10.3892/etm.2013.1145

Isolation and characterization of serum albumin from Camelus dromedarius

Authors:
- Ajamaluddin Malik
- Abdulrahman Al-Senaidy
- Ewa Skrzypczak-Jankun
- Jerzy Jankun
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Affiliations: Protein Research Chair, Department of Biochemistry, College of Sciences, King Saud University, Riyadh 11451, Kingdom of Saudi Arabia, Urology Research Center, Department of Urology, The University of Toledo, Health Science Campus, Toledo, OH 43614, USA
Published online on: June 6, 2013 https://doi.org/10.3892/etm.2013.1145
Pages: 519-524

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Abstract

Serum albumin constitutes 35-50 mg/ml of plasma proteins and performs various physiological activities including the regulation of osmotic pressure on blood, maintaining buffering of the blood pH, carrying different fatty acids and other small molecules, such as bilirubin, hormones, drugs and metal ions, as well as participating in immunological responses. Serum albumin is an extensively used protein in biotechnological and pharmaceutical industries. The camel (Camelus dromedarius) is well tailored to successfully survive in extremely hot and dry climates. Plasma osmolality in the camel increases during water‑deprived conditions. In such circumstances serum albumin is crucial in the regulation of blood pressure. The study of biochemical, biophysical and immunological aspects of camel serum albumin (CSA) are likely to provide molecular insights into camel physiology and may render it an alternative to human serum albumin (HSA) and bovine serum albumin (BSA) in all cases. However, these proteins are currently not available or cannot be utilized due to a variety of considerations. In this study, 12 mg of highly pure CSA was obtained from 1 ml plasma. Coomassie Brilliant Blue staining of SDS-PAGE yielded one band and RP-HPLC results revealed a single sharp peak, indicating homogenous preparation of the CSA. The charge/mass ratio and surface hydrophobicity of the CSA was similar to that of BSA. Mass spectrometry analysis of the purified protein confirmed the identity of CSA.

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1.	Lundsgaard-Hansen P: Physiology and pathophysiology of colloid osmotic pressure and albumin metabolism. Curr Stud Hematol Blood Transfus. 53:1–17. 1986.PubMed/NCBI
2.	Prajapati KD, Sharma SS and Roy N: Current perspectives on potential role of albumin in neuroprotection. Rev Neurosci. 22:355–363. 2011. View Article : Google Scholar : PubMed/NCBI
3.	Georgiou HM, Rice GE and Baker MS: Proteomic analysis of human plasma: failure of centrifugal ultrafiltration to remove albumin and other high molecular weight proteins. Proteomics. 1:1503–1506. 2001. View Article : Google Scholar : PubMed/NCBI
4.	Jiang L, He L and Fountoulakis M: Comparison of protein precipitation methods for sample preparation prior to proteomic analysis. J Chromatogr A. 1023:317–320. 2004. View Article : Google Scholar : PubMed/NCBI
5.	Olver CS, Webb TL, Long LJ, Scherman H and Prenni JE: Comparison of methods for depletion of albumin and IgG from equine serum. Vet Clin Pathol. 39:337–345. 2010. View Article : Google Scholar : PubMed/NCBI
6.	Kim SH, Kim UK, Lee WS, et al: Albumin-like protein is the major protein constituent of luminal fluid in the human endolymphatic sac. PLoS One. 6:e216562011. View Article : Google Scholar : PubMed/NCBI
7.	Wiig H, Reed RK and Tenstad O: Interstitial fluid pressure, composition of interstitium, and interstitial exclusion of albumin in hypothyroid rats. Am J Physiol Heart Circ Physiol. 278:H1627–H1639. 2000.PubMed/NCBI
8.	Shaklai N, Garlick RL and Bunn HF: Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J Biol Chem. 259:3812–3817. 1984.PubMed/NCBI
9.	Spector AA: Fatty acid binding to plasma albumin. J Lipid Res. 16:165–179. 1975.PubMed/NCBI
10.	Ashbrook JD, Spector AA, Santos EC and Fletcher JE: Long chain fatty acid binding to human plasma albumin. J Biol Chem. 250:2333–2338. 1975.PubMed/NCBI
11.	Sargent TD, Jagodzinski LL, Yang M and Bonner J: Fine structure and evolution of the rat serum albumin gene. Mol Cell Biol. 1:871–883. 1981.
12.	Gibbs PE and Dugaiczyk A: Origin of structural domains of the serum-albumin gene family and a predicted structure of the gene for vitamin D-binding protein. Mol Biol Evol. 4:364–379. 1987.PubMed/NCBI
13.	Fanali G, Ascenzi P, Bernardi G and Fasano M: Sequence analysis of serum albumins reveals the molecular evolution of ligand recognition properties. J Biomol Struct Dyn. 29:691–701. 2012. View Article : Google Scholar : PubMed/NCBI
14.	Bujacz A: Structures of bovine, equine and leporine serum albumin. Acta Crystallogr D Biol Crystallogr. 68:1278–1289. 2012. View Article : Google Scholar : PubMed/NCBI
15.	Luo Z, Shi X, Hu Q, Zhao B and Huang M: Structural evidence of perfluorooctane sulfonate transport by human serum albumin. Chem Res Toxicol. 25:990–992. 2012. View Article : Google Scholar : PubMed/NCBI
16.	Curry S, Mandelkow H, Brick P and Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 5:827–835. 1998. View Article : Google Scholar : PubMed/NCBI
17.	Sugio S, Kashima A, Mochizuki S, Noda M and Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 12:439–446. 1999. View Article : Google Scholar
18.	Maruyama T, Katoh S, Nakajima M and Nabetani H: Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotechnol Bioeng. 75:233–238. 2001. View Article : Google Scholar : PubMed/NCBI
19.	Carter DC and Ho JX: Structure of serum albumin. Adv Protein Chem. 45:153–203. 1994. View Article : Google Scholar : PubMed/NCBI
20.	Phillips A, Shaper AG and Whincup PH: Association between serum albumin and mortality from cardiovascular disease, cancer, and other causes. Lancet. 2:1434–1436. 1989. View Article : Google Scholar : PubMed/NCBI
21.	Nicholson JP, Wolmarans MR and Park GR: The role of albumin in critical illness. Br J Anaesth. 85:599–610. 2000. View Article : Google Scholar : PubMed/NCBI
22.	Singh-Zocchi M, Andreasen A and Zocchi G: Osmotic pressure contribution of albumin to colloidal interactions. Proc Natl Acad Sci USA. 96:6711–6715. 1999.PubMed/NCBI
23.	Stewart AJ, Blindauer CA, Berezenko S, Sleep D and Sadler PJ: Interdomain zinc site on human albumin. Proc Natl Acad Sci USA. 100:3701–3706. 2003. View Article : Google Scholar
24.	Hu W, Luo Q, Wu K, et al: The anticancer drug cisplatin can cross-link the interdomain zinc site on human albumin. Chem Commun (Camb). 47:6006–6008. 2011. View Article : Google Scholar : PubMed/NCBI
25.	Vorum H: Reversible ligand binding to human serum albumin. Theoretical and clinical aspects. Dan Med Bull. 46:379–399. 1999.PubMed/NCBI
26.	Chuang VT, Kragh-Hansen U and Otagiri M: Pharmaceutical strategies utilizing recombinant human serum albumin. Pharm Res. 19:569–577. 2002. View Article : Google Scholar : PubMed/NCBI
27.	Fasano M, Curry S, Terreno E, et al: The extraordinary ligand binding properties of human serum albumin. IUBMB Life. 57:787–796. 2005. View Article : Google Scholar : PubMed/NCBI
28.	Buckow R, Wendorff J and Hemar Y: Conjugation of bovine serum albumin and glucose under combined high pressure and heat. J Agric Food Chem. 59:3915–3923. 2011. View Article : Google Scholar : PubMed/NCBI
29.	Xiao J, Wu M, Kai G, Wang F, Cao H and Yu X: ZnO-ZnS QDs interfacial heterostructure for drug and food delivery application: enhancement of the binding affinities of flavonoid aglycones to bovine serum albumin. Nanomedicine. 7:850–858. 2011. View Article : Google Scholar
30.	Yang M, Hoppmann S, Chen L and Cheng Z: Human serum albumin conjugated biomolecules for cancer molecular imaging. Curr Pharm Des. 18:1023–1031. 2012. View Article : Google Scholar : PubMed/NCBI
31.	Zhi J, Teller SB, Satoh H, Koss-Twardy SG and Luke DR: Influence of human serum albumin content in formulations on the bioequivalency of interferon alfa-2a given by subcutaneous injection in healthy male volunteers. J Clin Pharmacol. 35:281–284. 1995. View Article : Google Scholar : PubMed/NCBI
32.	Otsubo E and Takei T: Characterization of the surface activity of a synthetic surfactant with albumin. Biol Pharm Bull. 25:1519–1523. 2002. View Article : Google Scholar : PubMed/NCBI
33.	Basrur V, Yang F, Kushimoto T, et al: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2:69–79. 2003. View Article : Google Scholar : PubMed/NCBI
34.	Angal S and Dean PD: The effect of matrix on the binding of albumin to immobilized Cibacron Blue. Biochem J. 167:301–303. 1977.PubMed/NCBI
35.	Leatherbarrow RJ and Dean PD: Studies on the mechanism of binding of serum albumins to immobilized cibacron blue F3G A. Biochem J. 189:27–34. 1980.PubMed/NCBI
36.	Metcalf EC, Crow B and Dean PD: The effect of ligand presaturation on the interaction of serum albumins with an immobilized Cibacron Blue 3G-A studied by affinity gel electrophoresis. Biochem J. 199:465–472. 1981.PubMed/NCBI
37.	Malik A, Rudolph R and Sohling B: A novel fusion protein system for the production of native human pepsinogen in the bacterial periplasm. Protein Expr Purif. 47:662–671. 2006. View Article : Google Scholar : PubMed/NCBI
38.	Girard M, Bietlot HP, Mousseau N, Cyr TD and Ethier JC: Use of capillary electrophoresis for the characterization of human serum albumin heterogeneity. Biomed Chromatogr. 12:183–184. 1998. View Article : Google Scholar : PubMed/NCBI
39.	Francis GL: Albumin and mammalian cell culture: implications for biotechnology applications. Cytotechnology. 62:1–16. 2010. View Article : Google Scholar : PubMed/NCBI