caa a22 4500 467978956 CHVBK 20180323112514.0 cr unu---uuuuu 170328e19901101xx s 000 0 eng 10.1007/BF01974691 doi (NATIONALLICENCE)springer-10.1007/BF01974691 Interaction of methylmercury compounds with albumin [Elektronische Daten] [Akira Yasutake, Kimiko Hirayama, Masayasu Inoue] The nature of interaction between bovine serum albumin (BSA) and methylmercurial compounds has been investigated by ultrafiltration analysis. Four types of BSA samples, mercaptalbumin, its mixed disulfides with glutathione (GSH) andl-cysteine (CySH), and the S-carbami-domethylated derivative, were used for binding assays with methylmercury (MM) chloride (MMC) and three kinds of MM mercaptides of low molecular weight thiols, GSH (GS-MM), CySH (CyS-MM) and cysteinylglycine (CG-MM). Among various ligands tested, MMC showed the highest affinity for all BSA species, and the BSA-bound fraction of the ligand did not change with ligand/protein ratio. MMC strongly and stoichiometrically bound to mercaptalbumin even at a molar ratio of 1∶1. In contrast, the albumin bound fractions of three other MM ligands increased with concomitant decrease in ligand/protein ratio and with time except for the alkylated albumin, the highest binding being shown by mercaptalbumin. Binding of S-2-nitrophenyl-glutathione, a GSH analog with a hydrophobic S-substituent, to albumin species occurred similarly to that of GS-MM. However, GSH and oxidized glutathione (GSSG) interacted differently with albumin; mercaptalbumin showed the lowest affinity for GSH, and GSSG scarcely interacted with all BSA species. These results suggest that the sulfhydryl group at Cys-34 is not the only site of BSA that interacts with MM compounds and that albumin interacts preferentially with the hydrophobic domains of a mercurial ligand rather than its hydrophilic peptide moiety. Springer-Verlag, 1990 Methylmercury nationallicence Bovine serum albumin nationallicence Mercaptide nationallicence Glutathione nationallicence Mixed disulfide nationallicence Alb-SH : mercaptalbumin nationallicence Alb-SSCy : cysteine-mixed disulfide of albumin nationallicence Alb-SSG : glutathione-mixed disulfide of albumin nationallicence Alb-SCAM : S-carbamidomethylalbumin nationallicence CG-MM : S-methylmercury cysteinylglycine nationallicence CyS-MM : S-methylmercury cysteine nationallicence GS-MM : S-methylmercury glutathione nationallicence GS-NP : S-o-nitrophenyl glutathione nationallicence MM : methylmercury nationallicence MMC : methylmercury chloride nationallicence Yasutake Akira Biochemistry Section, National Institute for Minamata Disease, Minamata City, 867, Kumamoto aut Hirayama Kimiko Kumamoto University College of Medical Science, 4-24-1 Kuhonji, 862, Kumamoto aut Inoue Masayasu Department of Biochemistry, Kumamoto University Medical School, 2-2-1 Honjo, 860, Kumamoto, Japan aut Archives of Toxicology Springer-Verlag 64/8(1990-11-01), 639-643 0340-5761 64:8<639 1990 64 204 https://doi.org/10.1007/BF01974691 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01974691 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yasutake Akira Biochemistry Section, National Institute for Minamata Disease, Minamata City, 867, Kumamoto aut NATIONALLICENCE 700 1- Hirayama Kimiko Kumamoto University College of Medical Science, 4-24-1 Kuhonji, 862, Kumamoto aut NATIONALLICENCE 700 1- Inoue Masayasu Department of Biochemistry, Kumamoto University Medical School, 2-2-1 Honjo, 860, Kumamoto, Japan aut NATIONALLICENCE 773 0- Archives of Toxicology Springer-Verlag 64/8(1990-11-01), 639-643 0340-5761 64:8<639 1990 64 204 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer