Isolation and characterization of bovine factor VII.

Abstract:

:Factor VII (proconvertin) has been purified approximately 5 x 10(5)-fold from bovine plasma with an overall yield of 30%. The isolation procedure involves barium sulfate adsorption and elution, DEAE-Sephadex batchwise adsorption and elution, benzamidine-agarose column chromatography, heparin-agarose column chromatography, and preparative polyacrylamide gel disc electrophoresis. The final product was homogeneous when examined by gel electrophoresis in the presence of sodium dodecyl sulfate. A minimal molecular weight of 45,500 was determined by sedimentation equilibrium. The molecular weight estimated by sodium dodecyl sulfate gel electrophoresis was 54,000. Factor VII is composed of a single polypeptide chain possessing an amino-terminal sequence of Ala-Asn-Gly-Phe-Leu-. The amino acid and carbohydrate compositions of factor VII are also reported.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kisiel W,Davie EW

doi

10.1021/bi00693a023

subject

Has Abstract

pub_date

1975-11-04 00:00:00

pages

4928-34

issue

22

eissn

0006-2960

issn

1520-4995

journal_volume

14

pub_type

杂志文章