Purification of human brain tissue factor

G. J. Broze, J. E. Leykam, B. D. Schwartz, J. P. Miletich

Research output: Contribution to journalArticlepeer-review

94 Scopus citations

Abstract

Tissue factor (factor III) is a lipoprotein cofactor which markedly enhances the catalytic effect of coagulation factor VII(a) upon factors IX and X. Human tissue factor apoprotein was purified 53,000-fold to homogeneity from brain using acetone delipidation, Triton X-100 extraction, and affinity chromatography upon factor VII-agarose. The purified apoprotein has an apparent molecular weight of 44,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, an amino acid composition similar to bovine brain tissue factor, and an NH2-terminal amino acid sequence of Ser-X-Asn-Thr-Val-Ala-Val-Tyr-X-Tyr-X-Leu-Lys-(Ser)-Lys-Asn-Phe. Optimal relipidation of the tissue factor apoprotein was associated with a 5000-fold enhancement of clotting activity and occurred at a phospholipid/apoprotein (w/w) ratio of > 600.

Original languageEnglish
Pages (from-to)10917-10920
Number of pages4
JournalJournal of Biological Chemistry
Volume260
Issue number20
StatePublished - 1985

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