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- W62963640 abstract "Publisher Summary This chapter explores metal ion binding properties of nitrated S-100b protein. S-100b protein exists as a dimer of 21,000 molecular weight in native solvents. The S-100b protein polypeptide chain (β-subunit) consists of 91 amino acid residues and contains a typical EF-hand type calcium-binding region located between residues 61 and 72. Tetranitromethane (TNM) under controlled conditions can be used specifically to modify tyrosine residues in proteins. The absorption spectrum of nitrated S-100b was similar to that of native S-100b. Tyrosine CD bands were located at 284 and 278 nm, and the phenylalanine CD bands were positioned at 268.5 and 262 nm. Even though the modified protein binds Ca2+ it differs significantly from the native protein in the manner in which it responds to Ca2+. Ca2+ and Zn2+ ions are believed to bind at different sites on the polypeptide chain based on our earlier spectroscopic studies with the apoprotein. Because the Zn2+ binding site, possibly involving histidine 15 or 25, is very close to tyrosine 17, the nitrated S-100b changes were monitored in the environment of tyrosine as a result of Zn2+ addition." @default.
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- W62963640 date "1987-01-01" @default.
- W62963640 modified "2023-09-27" @default.
- W62963640 title "METAL ION BINDING PROPERTIES OF NITRATED S-100b PROTEIN Supported by Medical Research Council of Canada." @default.
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- W62963640 doi "https://doi.org/10.1016/b978-0-12-521040-9.50066-8" @default.
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