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: A specific immune response was defined for each compound belonging to the same metabolic pathway, and the cross‐reactivity ratios were found to be smallest for the most immunoreactive conjugates.
Abstract: Antisera were raised against tryptophan, 5-hydroxytryptophan, 5-hydroxytryptamine, 5-methoxytryptophan, and 5-methoxytryptamine, by conjugating each molecule to bovine serum albumin and to human serum albumin via glutaraldehyde, in such a way as to preserve the original part. Antibody specificity was tested with the enzyme-linked immunosorbent assay method. The specificity of each anti-indolealkylamine-glutaraldehyde antibody was established with competition experiments by using an adsorbed immunogenic conjugate and indolealkylamines either free or conjugated with poly-L-lysine. The nonconjugated compounds were poorly recognized. In the same way, the nonreduced conjugates always appeared less immunoreactive than the reduced ones. Calculated from the specificity study of each antiserum, the cross-reactivity ratios were found to be smallest for the most immunoreactive conjugates. Thus, a specific immune response was defined for each compound belonging to the same metabolic pathway.
91 citations
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TL;DR: In this article, the interaction of 7-aminocoumarins with human serum albumin (HSA) was studied by using fluorescence spectroscopic technique and modeling studies.
91 citations
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91 citations
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91 citations
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TL;DR: The Hummel-Dreyer size-exclusion high-performance liquid chromatographic method for the determination of protein binding parameters has been improved and automated by use of an internal surface reversed-phase (ISRP) column and a computer-controlled mobile-phase delivery system with low volume syringe mixing.
Abstract: The Hummel-Dreyer size-exclusion high-performance liquid chromatographic method for the determination of protein binding parameters has been improved and automated by use of an internal surface reversed-phase (ISRP) column (5 cm X 4.6 mm) and a computer-controlled mobile-phase delivery system with low volume syringe mixing. The high-efficiency ISRP columns, which are nonadsorptive and exclusionary to serum proteins but allow partitioning of small molecules with an internal peptide bonded phase, maintain high performance after many injections of human serum albumin (HSA), enable the use of short columns, and provide for the resolution of primary ligand from protein binding displacers. The modified Hummel-Dreyer high-performance liquid chromatographic method was demonstrated by the determination of binding parameters for warfarin-HSA in phosphate buffer, which were found to be n1 = 1.0, n2 = 2.1, K1 = 3.30 X 10(5) M-1, and K2 = 2.03 X 10(4) M-1. The necessary sequence of chromatographic experiments was repeated 4 times at 18 separate warfarin mobile phase concentrations. Each automated sequence required 8 h to complete. The parameters were measured with a precision of less than 10% relative standard deviation.
91 citations