Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis.

Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Research Abstract Details 

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Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Abstract Text:

H Atoda,T Morita,

Blood coagulation factor IX/factor X-binding protein (IX/X-bp) is a two-chain anticoagulant protein that was isolated from the venom of Trimeresurus flavoviridis. The amino acid sequence of IX/X-bp is homologous to the sequences of C-type lectin-like proteins, such as asialoglycoprotein receptor, tetranectin, and the low-affinity Fc epsilon receptor of immunoglobulin E. The amino acid composition and amino acid sequence of cystine-containing peptides, formed as a result of enzymatic digestion of CNBr-generated fragments of IX/X-bp, were analyzed to determine the location of the seven disulfide bridges in the protein. Three disulfide bridges in the A chain link Cys2 to Cys13, Cys30 to Cys127, and Cys102 to Cys119. Three disulfide bridges in the A chain link Cys2 to Cys13, Cys30 to Cys119, and Cys96 to Cys111. An interchain disulfide bond links Cys79 of the A chain and Cys75 of the B chain. The intrachain disulfide-bonding patterns of both the A and B chains of IX/X-bp are similar to those found in other C-type lectin-like proteins. We discuss in this report the sequence homology between IX/X-bp and other two-chain, C-type lectin-like proteins that have been isolated from snake venoms and we compare the S-S bonding patterns of proteins that are homologous to IX/X-bp.

Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Publishing Authors By Initials

H Atoda,T Morita,

For similar proteins: reptilian proteins research abstracts see: proteins: reptilian proteins research

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Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 113

Page Numbers: 159-63

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1993

Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Keywords Mesh Terms:

KEYWORDS: Reptilian Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. Information

Substance Name: factor IX-factor X-binding protein, Crot

Registry Number: 143012-00-4

Grant and Affiliation Information for Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis.

AFFILIATION: Department of Biochemistry, Meiji College of Pharmacy, Tokyo.

Country: JAPAN

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MEDLINETA: J Biochem

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