PURIFICATION AND PROPERTIES OF FACTOR-XIII FROM HUMAN PLACENTA

被引：16

作者：

DEBACKERROYER, C ^{[1
]}

TRAORE, F ^{[1
]}

MEUNIER, JC ^{[1
]}

机构：

[1] INST NATL AGRON PARIS GRIGNON,CTR GRIGNON,CHIM BIOL LAB,F-78850 THIVERVAL GRIGNON,FRANCE

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1992年 / 24卷 / 01期

关键词：

D O I：

10.1016/0020-711X(92)90234-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. FXIII was isolated and purified over 4000 fold from human placenta to apparent electrophoretic homogeneity by a new procedure including ethanol precipitation. DEAE-Cellulose, molecular sieving on Sephacryl S-300 and Phenyl-Sepharose chromatography. 2. Its pl was about 5.1. Under appropriate conditions, the incubation of FXIII in the presence of thrombin did not lead to inactivation cut in the polypeptidic chain. 3. FXIII was also activated by CaCl2 and, in a lesser extent, by other divalent cations like SrCl2, BaCl2 or MgCl2. 4. The binding of calcium to FXIII exhibited a negative cooperativity. 5. The activity-pH curve of the calcium-activated enzyme did not appear very different from that of the thrombin-activated enzyme.

引用

页码：91 / 97

页数：7

共 13 条

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