A unique membrane-bound, calcium-dependent endopeptidase with specificity toward paired basic residues in rat liver Golgi fractions

Kensaku Mizuno, Tomoko Nakamura, Hisayuki Matsuo

研究成果: Article査読

18 被引用数 (Scopus)

抄録

A unique calcium-dependent endopeptidase specifically cleaving on the carboxyl side of paired basic residues was partially purified from Golgi membrane fractions of rat liver. The enzyme, with optimal pH at around 6.0, hydrolyzes synthetic peptides corresponding to the amino-terminal sequences of proalbumin and proparathyroid hormone at the carboxyl sides of paired basic residues (Arg-Arg and Lys-Arg), but peptides corresponding to the amino-terminal sequences of proalbumin variants, in which Arg-Arg at the site of cleavage is replaced by Arg-Gln or His-Arg, are not affected by the enzyme. From its strict substrate specificity and inhibitory spectrum, this enzyme appears to be a novel endopeptidase distinct from trypsin and cathepsin B and may be physiologically involved in proprotein processing.

本文言語English
ページ(範囲)780-787
ページ数8
ジャーナルBiochemical and biophysical research communications
164
2
DOI
出版ステータスPublished - 1989 10月 31
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

フィンガープリント

「A unique membrane-bound, calcium-dependent endopeptidase with specificity toward paired basic residues in rat liver Golgi fractions」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル