COMPARISON OF AMINO-ACID SEQUENCE OF BOVINE COAGULATION FACTOR-IX (CHRISTMAS FACTOR) WITH THAT OF OTHER VITAMIN-K-DEPENDENT PLASMA-PROTEINS

被引:161
作者
KATAYAMA, K [1 ]
ERICSSON, LH [1 ]
ENFIELD, DL [1 ]
WALSH, KA [1 ]
NEURATH, H [1 ]
DAVIE, EW [1 ]
TITANI, K [1 ]
机构
[1] UNIV WASHINGTON, DEPT BIOCHEM, SEATTLE, WA 98195 USA
关键词
D O I
10.1073/pnas.76.10.4990
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The amino acid sequence of bovine blood coagulation Factor IX (Christmas Factor) is presented and compared with the sequences of other vitamin K-dependent plasma proteins and pancreatic trypsinogen. The 416-residue sequence of Factor IX was determined largely by automated Edman degradation of two large segments, containing 181 and 235 residues, isolated after activating Factor IX with a protease from Russell's viper venom. Subfragments of the two segments were produced by enzymatic digestion and by chemical cleavage of methionyl, tryptophyl, and asparaginyl-glycyl bonds. Comparison of the amino acid sequences of factor IX, Factor X, and Protein C demonstrates that they are homologous throughout. Their homology with prothrombin, however, is restricted to the amino-terminal region, which is rich in γ-carboxyglutamic acid, and the carboxyl-terminal region, which represents the catalytic domain of these proteins and corresponds to that of pancreatic serine proteases.
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页码:4990 / 4994
页数:5
相关论文
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