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- W2087986504 abstract "Paired basic residues are known as a typical site for proteolytic processing of precursors of bioactive peptides. By using a fluorogenic substrate Boc-Gln-Arg-Arg-MCA, a unique endoprotease exhibiting hydrolytic specificity toward the carboxyl side of paired basic residues was partially purified (about 4600-fold) from the membrane fraction of yeast Saccharomyces cerevisiae α-cells. The enzyme is a calcium-dependent thiol protease, with optimal pH at 7.0. It is a glycoprotein, with an apparent molecular weight of about 100,000–120,000. It cleaves fluorogenic substrates and a synthetic model peptide at the carboxyl side of paired basic residues. From its unique substrate specificity, this enzyme may be involved in precursor processing in vivo." @default.
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- W2087986504 date "1987-04-01" @default.
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- W2087986504 title "A membrane-bound, calcium-dependent protease in yeast α-cell cleaving on the carboxyl side of paired basic residues" @default.
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- W2087986504 doi "https://doi.org/10.1016/s0006-291x(87)80036-0" @default.
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