The feasibility of radiolabeling for human serum albumin (HSA) adsorption studies
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چکیده
منابع مشابه
The Feasibility of Radiolabeling for Human Serum Albumin (HSA) Adsorption Studies
Human serum albumin (HSA) was labeled in various ways and with different radioactive labels (Technetium-99m and Iodine-125). Characterization with electrophoresis on polyacryl gel and immunoelectrophoresis did not reveal differences between labeled and nonlabeled HSA. The release of the label from labeled proteins in phosphate buffer (pH 7.4) was studied as a function of time. IzSI-labeled prot...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
متن کاملMolecular Dynamics Simulation and Free Energy Studies on the Interaction of Salicylic Acid with Human Serum Albumin (HSA)
Human serum albumin (HSA) is the most abundant protein in the blood plasma. Molecular dynamics simulations of subdomain IIA of HSA and its complex with salicylic acid (SAL) were performed to investigate structural changes induced by the ligand binding. To estimate the binding affinity of SAL molecule to subdomains IB and IIA in HSA protein, binding free energies were calculated using the Molecu...
متن کاملthe effects of acetaminophen on human serum albumin (hsa)
thermal conformational changes in human serum albumin (hsa) in present with a 10 mm phosphate buffer, at ph=7 have been investigated via circular dichroism (cd) and uv spectroscopic methods. the results indicate that temperature in a range of 25oc to 55oc could induce a reversible conformational change in the structure of hsa. the hsa phase transition corresponds to the physiological and pathol...
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ژورنال
عنوان ژورنال: Journal of Colloid and Interface Science
سال: 1978
ISSN: 0021-9797
DOI: 10.1016/0021-9797(78)90194-7