Pathways to Blood Coagulation Product I Formation

Author:

SPAET THEODORE H.12,CINTRON JOSÉ13

Affiliation:

1. Department of Hematology, Laboratory Division, Montefiore Hospital, New York, N. Y.

2. Monte fibre Hospital, and Associate Professor of Pathology, Columbia University College of Physicians and Surgeons, New York, N. Y.

3. Montefiore Hospital, NewYork, N. Y.

Abstract

Abstract The basic reagent used was an eluate obtained from barium sulfate used to adsorb various sera. When this eluate was prepared from normal rabbit serum, it responded to treatment with coagulants from adsorbed plasma, with Stypven, or with 25 per cent sodium citrate to give products with similar if not identical properties. With each preparation a stable complex formed with cephalin which withstood washing, was relatively heat-stable, was inactivated by adsorbed serum, and which required factor V for optimal prothrombin conversion. In eluates prepared from human serum, normal activation occurred in the absence of factor IX, but was defective in the absence of factor X. A preparation of factor X purified by DEAE cellulose chromatography was activated by 25 per cent sodium citrate. It is suggested that product I, the product of Stypven activation, and autoprothrombin C represent similar or identical reagents; it is further suggested that factor X is their common precursor.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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1. Enzymology and the Blood Clotting Mechanism;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

2. The Prothrombin-Converting Complex;Biochemical Society Transactions;1977-10-01

3. Purification and Properties of Blood-coagulating Protease fromCephalosporiumsp.;Agricultural and Biological Chemistry;1977-02

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