Results 301 to 310 of about 1,355,358 (352)
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Adverse Reactions to Human Serum Albumin
Annals of Pharmacotherapy, 1993OBJECTIVE: To describe the adverse effects associated with human serum albumin (HSA) administration. DATA SOURCES: A MEDLINE search and bibliography scanning were used to identify pertinent review articles, clinical studies, and case reports. STUDY SELECTION: Emphasis was placed on reporting the results of human studies with the primary objective of ...
B J, Gales, B L, Erstad
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Further characterization of specific drug binding sites on human serum albumin.
Molecular Pharmacology, 1976The fluorescent probes 5-dimethylaminonaphthalene-1-sulfonamide and dansylsarcosine function as specific markers for two distinct binding sites for anionic drugs on human serum albumin (HSA). The binding of drugs to site I or II was detected by measuring
Gillian Sudlow, D. Birkett, D. Wade
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Albumin Máku: a New Variant of Human Serum Albumin
Nature, 1968AT least six different electrophoretic variants of human serum albumin have been found in man; three migrate more rapidly than normal and three less rapidly1,2. One of these, a rapidly migrating variant, occurs at a frequency of 5–30 per cent in several tribes of North American Indians3.
L R, Weitkamp, N A, Chagnon
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Phase I Comparability of Recombinant Human Albumin and Human Serum Albumin
The Journal of Clinical Pharmacology, 2005Recombinant human albumin (rHA) is a highly purified animal‐, virus‐, and prion‐free product developed as an alternative to human serum albumin (HSA), to which it is structurally equivalent. The present investigation compared the safety, tolerability, and pharmacokinetics/pharmacodynamics of rHA with HSA.
Dietrich, Bosse +6 more
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Human serum albumin as multifunctional nanocarrier for cancer therapy.
Journal of Pharmacy and Science, 2021F. Zeeshan +4 more
semanticscholar +1 more source
Pharmaceutical Strategies Utilizing Recombinant Human Serum Albumin
Pharmaceutical Research, 2002Gene manipulation techniques open up the possibility of making recombinant human serum albumin (rHSA) or mutants with desirable therapeutic properties and for protein fusion products. rHSA can serve as a carrier in synthetic heme protein, thus reversibly carrying oxygen.
Chuang, V.T. +2 more
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α‐Tocopherol binding to human serum albumin
BioFactors, 2013AbstractGiven the ability of human serum albumin (HSA) to bind hydrophobic ligands, the binding mode of α‐tocopherol, the most representative member of the vitamin E family, is reported. α‐Tocopherol binds to HSA withK$_{\rm d}^0$= (7.0 ± 3.0) × 10−6M (pH 7.2, 25.0°C).
Fanali, G. +4 more
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International Archives of Allergy and Immunology, 1986
Sera from patients undergoing hemodialysis with formaldehyde (F)-sterilized dialyzers were studied to determine if antibodies against F conjugated to human serum albumin (HSA) could be detected. F-human serum albumin (F-HSA) conjugates were prepared using ratios of F to HSA that did not precipitate the HSA.
R, Patterson +3 more
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Sera from patients undergoing hemodialysis with formaldehyde (F)-sterilized dialyzers were studied to determine if antibodies against F conjugated to human serum albumin (HSA) could be detected. F-human serum albumin (F-HSA) conjugates were prepared using ratios of F to HSA that did not precipitate the HSA.
R, Patterson +3 more
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Detection Methods and Research Progress of Human Serum Albumin
Critical Reviews in Analytical Chemistry, 2022Yu-Shun Yang +2 more
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