Proteolytic cleavage of vitamin K-dependent bovine plasma protein S by α-thrombin and plasma serine protease

Takashi Morita, Jun Mizuguchi, Shun-Ichiro Kawabata, Sadaaki Iwanaga

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

It is known that protein S, a vitamin K-dependent plasma protein, isolated from a human source, gives a closely spaced doublet on sodium dodecyl sulfate-polyacryl amide gel electrophoresis after reduction and that this heterogeneity in molecular size results from a limited proteolysis of protein S mediated by α-thrombin in human species. We found here that a-thrombin also rapidly converted single-chain bovine protein S to a nicked form, which consisted of the NH2 segment containing γ-carboxyglutamic acid and the COOH-terminal large segment bridged by a distilfide linkage(s). These two segments were isolated and chemically characterized after S-alkylation of the nicked protein S. The results suggest that the α-thrombin-catalyzed hydrolysis of protein S probably occurs at a peptide linkage (Arg-Ser) located in the NH2 portion. The conversion of single-chain protein S to the nicked form was also mediated by plasma kallikrein and plasmin, in addition to α-chymotrypsin and trypsin. However, the α-thrombin-catalyzed conversion did not occur when calcium ions were added to the reaction mixture.

Original languageEnglish
Pages (from-to)561-568
Number of pages8
JournalJournal of biochemistry
Volume99
Issue number2
DOIs
Publication statusPublished - Jan 1 1986

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Vitamin K
Protein S
Serine Proteases
Thrombin
Blood Proteins
Plasmas
Plasma Kallikrein
Proteolysis
Fibrinolysin
Alkylation
Electrophoresis
Amides
Sodium Dodecyl Sulfate
Hydrolysis
Gels
Ions
Calcium
Peptides
Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Proteolytic cleavage of vitamin K-dependent bovine plasma protein S by α-thrombin and plasma serine protease. / Morita, Takashi; Mizuguchi, Jun; Kawabata, Shun-Ichiro; Iwanaga, Sadaaki.

In: Journal of biochemistry, Vol. 99, No. 2, 01.01.1986, p. 561-568.

Research output: Contribution to journalArticle

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AB - It is known that protein S, a vitamin K-dependent plasma protein, isolated from a human source, gives a closely spaced doublet on sodium dodecyl sulfate-polyacryl amide gel electrophoresis after reduction and that this heterogeneity in molecular size results from a limited proteolysis of protein S mediated by α-thrombin in human species. We found here that a-thrombin also rapidly converted single-chain bovine protein S to a nicked form, which consisted of the NH2 segment containing γ-carboxyglutamic acid and the COOH-terminal large segment bridged by a distilfide linkage(s). These two segments were isolated and chemically characterized after S-alkylation of the nicked protein S. The results suggest that the α-thrombin-catalyzed hydrolysis of protein S probably occurs at a peptide linkage (Arg-Ser) located in the NH2 portion. The conversion of single-chain protein S to the nicked form was also mediated by plasma kallikrein and plasmin, in addition to α-chymotrypsin and trypsin. However, the α-thrombin-catalyzed conversion did not occur when calcium ions were added to the reaction mixture.

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