A putative prohormone processing protease in bovine adrenal medulla specifically cleaving in between Lys-Arg sequences

Kensaku Mizuno, Masayasu Kojima, Hisayuki Matsuo

研究成果: Article査読

42 被引用数 (Scopus)

抄録

Paired basic residues, particularly Lys-Arg, are known as a typical site for proteolytic processing of prohormones. In this study, we confirmed the presence of a novel protease exhibiting substrate specificity toward Lys-Arg sequence. It was partially purified from the soluble fraction of bovine adrenomedullary chromaffin granules by using an affinity chromatography on soybean trypsin inhibitor-Sepharose. The enzyme, with optimal pH around 7.5-9.5, is classified into a serine-protease family by its inhibition spectrum. The enzyme specifically cleaves in between the Lys-Arg bonds of the peptides related to proenkephalins, but the sequences of Arg-Arg, Arg-Lys and a single basic residue (Arg or Lys) in the substrates are not affected by the enzyme. The unique substrate specificity of the enzyme suggests that it is distinct from pancreatic trypsin and may be physiologically involved in proenkephalin processing.

本文言語English
ページ(範囲)884-891
ページ数8
ジャーナルBiochemical and biophysical research communications
128
2
DOI
出版ステータスPublished - 1985 4 30
外部発表はい

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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