TY - JOUR
T1 - A membrane-bound, calcium-dependent protease in yeast α-cell cleaving on the carboxyl side of paired basic residues
AU - Mizuno, Kensaku
AU - Nakamura, Tomoko
AU - Takada, Katsumi
AU - Sakakibara, Shumpei
AU - Matsuo, Hisayuki
PY - 1987/4/29
Y1 - 1987/4/29
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(87)80036-0
DO - 10.1016/S0006-291X(87)80036-0
M3 - Article
C2 - 3555496
AN - SCOPUS:0023229057
VL - 144
SP - 807
EP - 814
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -