Topic
Serum albumin
About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.
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130 citations
TL;DR: The thermal and structural properties of bovine serum albumin (BSA) were studied at different pH values, at different NaCl, lactose, sucrose, and glucose concentrations, and in the presence of cysteine, urea, NEM, and SDS as mentioned in this paper.
Abstract: The thermal and structural properties of bovine serum albumin (BSA) were studied at different pH values, at different NaCl, lactose, sucrose, and glucose concentrations, and in the presence of cysteine, urea, NEM, and SDS. Maximum thermal stability was observed at pH 5. Glucose had a greater stabilizing effect on the thermal denaturation of BSA than sucrose. Denaturation of BSA resulted in the loss of the 1654 cm-1 band attributed to α-helical structure and the rise of two bands at 1616 and 1684 cm-1 attributed to the formation of ordered non-native β-sheet structure associated with aggregation. SDS markedly increased the thermal stability of BSA and prevented aggregate formation. The greatest unfolding on heat treatment was observed in the presence of cysteine and the least in SDS. Keywords: Bovine serum albumin; differential scanning calorimetry; Fourier transform infrared spectroscopy; denaturation; gelation
130 citations
TL;DR: Both wild-type and mutant albumins promote the safe management of high micromolar zinc concentrations for cells in cultures, and the dynamics of the domain I/II interface are affected by Zn2+ binding, which induces cooperative allosteric effects related to those of the pH-dependent neutral-to-base transition.
130 citations
TL;DR: Fluorescence properties of albumin were altered by oxidation and, in patients with acute-on-chronic liver failure, by high plasma levels of bilirubin, providing evidence for a preferred binding of bilIRubin to the fully reduced form ofalbumin.
130 citations
TL;DR: It was concluded that colchicine may probably cause displacement of phenylbutazone from its complex with serum albumin (SA) and Static and dynamic quenching for the binary and ternary systems showed that phenyl butazone does not affect the complex formed between colchichine and BSA, and colchicaine has no effect on the Phe–BSA complex.
130 citations