Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: The docking results suggest that TP forms stable complex with HSA (Kb ∼ 104) and its primary binding site is located in subdomain IIA (Sudlow Site I), which indicated that the hydrophobic interactions play a main role in the binding of TP to human serum albumin.
76 citations
TL;DR: It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA.
Abstract: Commercially obtained pure human serum albumin (HSA) was shown to contain molecular aggregates and was significantly contaminated with Cu(II). A solution of commercial HSA was first passed through a Sephadex G-200 column to obtain pure monomeric HSA. The monomer of HSA was subsequently passed through Chelex-100 resin to free it from Cu(II). All Cu(II)-binding studies were conducted with monomeric and copper-free HSA. The first Cu(II)-binding site on HSA appears to be stronger than the second and the subsequent binding sites. Significant amounts of L-histidine and L-threonine were bound to HSA when Cu(II) was added in the form of Cu(II) – amino acid complexes. In the absence of Cu(II), free L-histidine or L-threonine do not bind to HSA at pH 7.4. It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA. In view of this finding, it appears that the equilibrium between HSA–Cu(II) and ...
76 citations
TL;DR: Computer mapping of the possible binding sites of mangiferin revealed the molecule to be bound in the large hydrophobic cavity of subdomain IIA, which led to changes in the conformation of HSA according to synchronous fluorescence spectra, FT-IR, UV-vis and CD data.
76 citations
TL;DR: The coloured sulfhydryl reagent, N-(4-dimethylamino-3,5-dinitrophenyl) maleimide (DDPM), has been synthesized and its reactions with cysteine and with the free SH groups of human and bovine serum albumin have been studied.
76 citations
TL;DR: The results indicate that the binding of bilirubin to the first binding site on albumin involves both hydrophobic and electrostatic forces and the results suggest that arginine, tyrosine and histidine residues are close to or located in the strong binding site.
Abstract: A number of derivatives of human serum albumin were prepared by chemical modification of native albumin with acetylsalicylic acid, succinic anhydride, maleic anhydride, methyl acetimidiate hydrochloride, N-acetylimidazole, acetic anhydride, tetranitromethane, diethylpyrocarbonate, glyoxal, ethyl diazoacetate and o-nitrophenylsulfenyl chloride. The conformational changes associated with the modification reactions were detected by Sephadex G-200 gel chromotography. The affinity of bilirubin for the modified albumins was estimated by the peroxidase method at a molar ratio of 0.5 bilirubin per albumin.
With increased unfolding of albumin, due to amino group modification, the affinity decreased. Acetylation of 22 or amidination of 52 amino groups or sulfenylation of the single tryptophan did not change the binding affinity significantly. Blocking of 10 arginine, 2 histidine or 8 tyrosine residues resulted in decreased affinity for bilirubin. The results indicate that the binding of bilirubin to the first binding site on albumin involves both hydrophobic and electrostatic forces. The results also suggest that arginine, tyrosine and histidine residues are close to or located in the strong binding site.
75 citations