Ljudski serumski albumin je najzastupljeniji protein u ljudskoj krvnoj plazmi. On se formira u jetri. Albumin sačinjava oko polovine krvnog serumskog proteina. On je rastvoran i monomeran. Albuminom se transportuju hormoni, masne kiseline, i druga jedinjenja, puferuje pH, i održava osmotski pritisak, i vrši niz drugih funkcija.[1][2]
Reference
↑Knox C, Law V, Jewison T, Liu P, Ly S, Frolkis A, Pon A, Banco K, Mak C, Neveu V, Djoumbou Y, Eisner R, Guo AC, Wishart DS (2011). „DrugBank 3.0: a comprehensive resource for omics research on drugs”. Nucleic Acids Res.39 (Database issue): D1035-41. DOI:10.1093/nar/gkq1126. PMC 3013709. PMID 21059682. edit
↑David S. Wishart, Craig Knox, An Chi Guo, Dean Cheng, Savita Shrivastava, Dan Tzur, Bijaya Gautam, and Murtaza Hassanali (2008). „DrugBank: a knowledgebase for drugs, drug actions and drug targets”. Nucleic Acids Res36 (Database issue): D901-6. DOI:10.1093/nar/gkm958. PMC 2238889. PMID 18048412. edit
Literatura
Komatsu T, Nakagawa A, Curry S, et al. (2009). „The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O(2) and CO binding to iron protoporphyrin IX”. Org. Biomol. Chem.7 (18): 3836–41. DOI:10.1039/b909794e. PMID 19707690.
Milojevic J, Raditsis A, Melacini G (2009). „Human Serum Albumin Inhibits Aβ Fibrillization through a "Monomer-Competitor" Mechanism”. Biophys. J.97 (9): 2585–94. DOI:10.1016/j.bpj.2009.08.028. PMC 2770600. PMID 19883602.
Silva AM, Hider RC (2009). „Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation”. Biochim. Biophys. Acta1794 (10): 1449–58. DOI:10.1016/j.bbapap.2009.06.003. PMID 19505594.
Otosu T, Nishimoto E, Yamashita S (2010). „Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy”. J. Biochem.147 (2): 191–200. DOI:10.1093/jb/mvp175. PMID 19884191.
Blindauer CA, Harvey I, Bunyan KE, et al. (2009). „Structure, Properties, and Engineering of the Major Zinc Binding Site on Human Albumin”. J. Biol. Chem.284 (34): 23116–24. DOI:10.1074/jbc.M109.003459. PMC 2755717. PMID 19520864.
Juárez J, Lápez SG, Cambán A, et al. (2009). „Influence of electrostatic interactions on the fibrillation process of human serum albumin”. J Phys Chem B113 (30): 10521–9. DOI:10.1021/jp902224d. PMID 19572666.
Fu BL, Guo ZJ, Tian JW, et al. (2009). „[Advanced glycation end products induce expression of PAI-1 in cultured human proximal tubular epithelial cells through NADPH oxidase dependent pathway]”. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi25 (8): 674–7. PMID 19664386.
Ascenzi P, di Masi A, Coletta M, et al. (2009). „Ibuprofen Impairs Allosterically Peroxynitrite Isomerization by Ferric Human Serum Heme-Albumin”. J. Biol. Chem.284 (45): 31006–17. DOI:10.1074/jbc.M109.010736. PMC 2781501. PMID 19734142.
Curry S (2002). „Beyond expansion: structural studies on the transport roles of human serum albumin”. Vox Sang.83 Suppl 1: 315–9. PMID 12617161.
Guo S, Shi X, Yang F, et al. (2009). „Structural basis of transport of lysophospholipids by human serum albumin”. Biochem. J.423 (1): 23–30. DOI:10.1042/BJ20090913. PMID 19601929.
de Jong PE, Gansevoort RT (2009). „Focus on microalbuminuria to improve cardiac and renal protection”. Nephron Clin Pract111 (3): c204–10; discussion c211. DOI:10.1159/000201568. PMID 19212124.
Page TA, Kraut ND, Page PM, et al. (2009). „Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids”. J Phys Chem B113 (38): 12825–30. DOI:10.1021/jp904475v. PMID 19711930.
Roche M, Rondeau P, Singh NR, et al. (2008). „The antioxidant properties of serum albumin”. FEBS Lett.582 (13): 1783–7. DOI:10.1016/j.febslet.2008.04.057. PMID 18474236.
Wyatt AR, Wilson MR (2010). „Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin”. J. Biol. Chem.285 (6): 3532–9. DOI:10.1074/jbc.M109.079566. PMC 2823492. PMID 19996109.
Cui FL, Yan YH, Zhang QZ, et al. (2010). „A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling”. J Mol Model16 (2): 255–62. DOI:10.1007/s00894-009-0548-4. PMID 19588173.
Caridi G, Dagnino M, Simundic AM, et al. (2010). „Albumin Benkovac (c.1175 A > G; p.Glu392Gly): a novel genetic variant of human serum albumin”. Transl Res155 (3): 118–9. DOI:10.1016/j.trsl.2009.10.001. PMID 20171595.
Deeb O, Rosales-Hernández MC, Gámez-Castro C, et al. (2010). „Exploration of human serum albumin binding sites by docking and molecular dynamics flexible ligand-protein interactions”. Biopolymers93 (2): 161–70. DOI:10.1002/bip.21314. PMID 19785033.
Karahan SC, Koramaz I, Altun G, et al. (2010). „Ischemia-modified albumin reduction after coronary bypass surgery is associated with the cardioprotective efficacy of cold-blood cardioplegia enriched with N-acetylcysteine: a preliminary study”. Eur Surg Res44 (1): 30–6. DOI:10.1159/000262324. PMID 19955769.
Jin C, Lu L, Zhang RY, et al. (2009). „Association of serum glycated albumin, C-reactive protein and ICAM-1 levels with diffuse coronary artery disease in patients with type 2 diabetes mellitus”. Clin. Chim. Acta408 (1–2): 45–9. DOI:10.1016/j.cca.2009.07.003. PMID 19615354.
Spoljašnje veze
Ljudski serumski albumin na Wikimedijinoj ostavi
Human serum albumin
Human Albumin structure in the Protein data bank
Human Albumin information in the Swis-Prot/TrEMBL database
Human Serum Albumin Arhivirano 2006-04-24 na Wayback Machine-u on the Human Protein Reference Database Arhivirano 2006-04-24 na Wayback Machine-u