Binding of mercury(II) to protein thiol groups: a study of proteinase K and carboxypeptidase Y

Autor:	Sven Bagger, Breddam K, Byberg Br
Rok vydání:	1991
Předmět:	Anions Magnetic Resonance Spectroscopy Saccharomyces cerevisiae Proteins Serine Proteinase Inhibitors Stereochemistry Protein Conformation Cathepsin A Carboxypeptidases Saccharomyces cerevisiae Biochemistry Inorganic Chemistry Sulfhydryl Compounds chemistry.chemical_classification biology Chemistry Serine Endopeptidases Potassium Iodide Chemical modification Nuclear magnetic resonance spectroscopy Mercury Proteinase K Carboxypeptidase Dissociation constant Enzyme Activation Kinetics Enzyme biology.protein Thiol CN-group Mitosporic Fungi Endopeptidase K Protein Binding
Zdroj:	Journal of inorganic biochemistry. 42(2)
ISSN:	0162-0134
Popis:	Chemically modified enzymes have been prepared by incorporating an -Hg-L group into proteinase K and carboxypeptidase Y at the thiol groups of Cys-73 and Cys-341, respectively (L = CN − or I − ). The -S-Hg- 13 CN group has been applied as a spectroscopic label for carbon-13 NMR spectroscopy.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34e8556a72f2c42aa01b7a77494a3e9a https://pubmed.ncbi.nlm.nih.gov/1856724 Zobrazit plný text záznamu