Staphylocoagulase-binding region in human prothrombin

Shun-Ichiro Kawabata, Takashi Morita, Sadaaki Iwanaga, Hideo Igarashi

研究成果: ジャーナルへの寄稿記事

34 引用 (Scopus)

抄録

A staphylocoagulase-binding region in human prothrombin was studied by utilizing several fragments prepared from prothrombin by limited proteolysis. Bovine prothrombin, prethrombin 1, prethrombin 2, and human diisopropylphosphorylated α-thrombin strongly inhibited formation of the complex ("staphylothrombin") between human prothrombin and staphylocoagulase, but bovine prothrombin fragment 1 and fragment 2 had no effect on the complex formation, indicating that the binding region of human prothrombin for staphylocoagulase is located in the prethrombin 2 molecule. To identify further the staphylocoagulase-binding region, human α-thrombin was cleaved into the NH2-terminal large fragment (Mr = 26, 000) and the COOH-terminal fragment (Mr = 16,000) by porcine pancreatic elastase. Of these fragments, the COOH-terminal fragment, which includes Asn-200 to the COOH-terminal end of the a-thrombin molecule, partially inhibited the complex formation between staphylocoagulase and human prothrombin. In contrast, the NH2-terminal large fragment did not show any inhibitory effect on the staphylo thrombin formation. These results suggest that the staphylocoagulase interacts with human prothrombin through the COOH-terminal region of α-thrombin B chain. Other plasma proteins, factor X, factor IX, protein C, protein S, protein Z, all of which are structurally similar to prothrombin, did not inhibit the staphylothrombin formation at all, indicating that a specific interaction site with staphylocoagulase is contained only in the prothrombin molecule.

元の言語英語
ページ(範囲)325-331
ページ数7
ジャーナルJournal of biochemistry
97
発行部数1
DOI
出版物ステータス出版済み - 1 1 1985

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Coagulase
Prothrombin
Thrombin
Molecules
Proteolysis
Factor X
Factor IX
Pancreatic Elastase
Protein S
Protein C
Blood Proteins
Swine

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Staphylocoagulase-binding region in human prothrombin. / Kawabata, Shun-Ichiro; Morita, Takashi; Iwanaga, Sadaaki; Igarashi, Hideo.

:: Journal of biochemistry, 巻 97, 番号 1, 01.01.1985, p. 325-331.

研究成果: ジャーナルへの寄稿記事

Kawabata, Shun-Ichiro ; Morita, Takashi ; Iwanaga, Sadaaki ; Igarashi, Hideo. / Staphylocoagulase-binding region in human prothrombin. :: Journal of biochemistry. 1985 ; 巻 97, 番号 1. pp. 325-331.
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abstract = "A staphylocoagulase-binding region in human prothrombin was studied by utilizing several fragments prepared from prothrombin by limited proteolysis. Bovine prothrombin, prethrombin 1, prethrombin 2, and human diisopropylphosphorylated α-thrombin strongly inhibited formation of the complex ({"}staphylothrombin{"}) between human prothrombin and staphylocoagulase, but bovine prothrombin fragment 1 and fragment 2 had no effect on the complex formation, indicating that the binding region of human prothrombin for staphylocoagulase is located in the prethrombin 2 molecule. To identify further the staphylocoagulase-binding region, human α-thrombin was cleaved into the NH2-terminal large fragment (Mr = 26, 000) and the COOH-terminal fragment (Mr = 16,000) by porcine pancreatic elastase. Of these fragments, the COOH-terminal fragment, which includes Asn-200 to the COOH-terminal end of the a-thrombin molecule, partially inhibited the complex formation between staphylocoagulase and human prothrombin. In contrast, the NH2-terminal large fragment did not show any inhibitory effect on the staphylo thrombin formation. These results suggest that the staphylocoagulase interacts with human prothrombin through the COOH-terminal region of α-thrombin B chain. Other plasma proteins, factor X, factor IX, protein C, protein S, protein Z, all of which are structurally similar to prothrombin, did not inhibit the staphylothrombin formation at all, indicating that a specific interaction site with staphylocoagulase is contained only in the prothrombin molecule.",
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AB - A staphylocoagulase-binding region in human prothrombin was studied by utilizing several fragments prepared from prothrombin by limited proteolysis. Bovine prothrombin, prethrombin 1, prethrombin 2, and human diisopropylphosphorylated α-thrombin strongly inhibited formation of the complex ("staphylothrombin") between human prothrombin and staphylocoagulase, but bovine prothrombin fragment 1 and fragment 2 had no effect on the complex formation, indicating that the binding region of human prothrombin for staphylocoagulase is located in the prethrombin 2 molecule. To identify further the staphylocoagulase-binding region, human α-thrombin was cleaved into the NH2-terminal large fragment (Mr = 26, 000) and the COOH-terminal fragment (Mr = 16,000) by porcine pancreatic elastase. Of these fragments, the COOH-terminal fragment, which includes Asn-200 to the COOH-terminal end of the a-thrombin molecule, partially inhibited the complex formation between staphylocoagulase and human prothrombin. In contrast, the NH2-terminal large fragment did not show any inhibitory effect on the staphylo thrombin formation. These results suggest that the staphylocoagulase interacts with human prothrombin through the COOH-terminal region of α-thrombin B chain. Other plasma proteins, factor X, factor IX, protein C, protein S, protein Z, all of which are structurally similar to prothrombin, did not inhibit the staphylothrombin formation at all, indicating that a specific interaction site with staphylocoagulase is contained only in the prothrombin molecule.

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