The amino acid sequence of the procoagulant- and prothrombin-binding domain isolated from staphylocoagulase

Shun-Ichiro Kawabata, T. Miyata, T. Morita, S. Iwanaga, H. Igarashi

研究成果: ジャーナルへの寄稿記事

19 引用 (Scopus)

抄録

The primary structure of the procoagulant- and prothrombin-binding domains, the 43- and 30-kDa fragments previously isolated from staphylocoagulase, has been determined by sequencing peptides derived from various chemical (CNBr and 2-(2-nitro-phenylsulfenyl)-3-methyl-3-bromoindolenine) and enzymatic (trypsin and α-chymotrypsin) cleavages. Carboxypeptidase Y was also used to deduce the COOH-terminal sequence. The 43-kDa fragment contained 324 amino acids and had a calculated molecular weight of 38,098. It included the entire structure of the 30-kDa fragment located in the COOH-terminal portion (positions 126-324). The 43-kDa fragment had an unusual amino acid composition based on the sequence, in which the sum of Asp (28 residues), Asn (22), Glu (35), Gln (9), and Lys (52) residues accounted for more than 45% of the total. In addition, the frequent occurrence of repetitions of the various kinds of dipeptides was found along the whole sequence. Structural comparison of the NH2-terminal portion of the 43-kDa fragment of staphylocoagulase with that of streptokinase did not reveal any obvious sequence homologies. There was also no sequence homology with that of trypsin, α-chymotrypsin, and elastase.

元の言語英語
ページ(範囲)527-531
ページ数5
ジャーナルJournal of Biological Chemistry
261
発行部数2
出版物ステータス出版済み - 5 28 1986

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Coagulase
Prothrombin
Sequence Homology
Amino Acid Sequence
Cathepsin A
Amino Acids
Streptokinase
Dipeptides
Pancreatic Elastase
Molecular Weight
Molecular weight
Peptides
Chemical analysis
trypsin drug combination chymotrypsin

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

The amino acid sequence of the procoagulant- and prothrombin-binding domain isolated from staphylocoagulase. / Kawabata, Shun-Ichiro; Miyata, T.; Morita, T.; Iwanaga, S.; Igarashi, H.

:: Journal of Biological Chemistry, 巻 261, 番号 2, 28.05.1986, p. 527-531.

研究成果: ジャーナルへの寄稿記事

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abstract = "The primary structure of the procoagulant- and prothrombin-binding domains, the 43- and 30-kDa fragments previously isolated from staphylocoagulase, has been determined by sequencing peptides derived from various chemical (CNBr and 2-(2-nitro-phenylsulfenyl)-3-methyl-3-bromoindolenine) and enzymatic (trypsin and α-chymotrypsin) cleavages. Carboxypeptidase Y was also used to deduce the COOH-terminal sequence. The 43-kDa fragment contained 324 amino acids and had a calculated molecular weight of 38,098. It included the entire structure of the 30-kDa fragment located in the COOH-terminal portion (positions 126-324). The 43-kDa fragment had an unusual amino acid composition based on the sequence, in which the sum of Asp (28 residues), Asn (22), Glu (35), Gln (9), and Lys (52) residues accounted for more than 45{\%} of the total. In addition, the frequent occurrence of repetitions of the various kinds of dipeptides was found along the whole sequence. Structural comparison of the NH2-terminal portion of the 43-kDa fragment of staphylocoagulase with that of streptokinase did not reveal any obvious sequence homologies. There was also no sequence homology with that of trypsin, α-chymotrypsin, and elastase.",
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T1 - The amino acid sequence of the procoagulant- and prothrombin-binding domain isolated from staphylocoagulase

AU - Kawabata, Shun-Ichiro

AU - Miyata, T.

AU - Morita, T.

AU - Iwanaga, S.

AU - Igarashi, H.

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