Biomedical subjects

M C DRUMMOND

Publications and source records attributed to M C DRUMMOND.

At least 19 recordsLinked to original sources

PubMed1963

FIBRINOGEN CLOTTING AND FIBRINO-PEPTIDE FORMATION BY STAPHYLOCOAGULASE AND THE COAGULASE-REACTING FACTOR.

Drummond, Margaret C. (Emory University, Atlanta, Ga.) and Morris Tager. Fibrinogen clotting and fibrino-peptide formation by staphylocoagulase and the coagulase-reacting factor. J. Bacteriol. 85:628-635. 1963.-The mechanism of fibrinogen clotting by staphylocoagulase and the coagulase-reacting factor (CRF) was studied from the standpoint of the products of the reaction, and compared with thrombin clotting of fibrinogen. Both clotting principles effect clotting with the release of nonprotein nitrogenous material, which can be resolved into three peptides by Dowex-50 chromatography. On the basis of the sedimentation constants, electrophoretic mobilities, and end-group analyses of these peptides, it appears that the products of fibrinogen clotting by coagulase-CRF and by thrombin are similar.

Coagulase↗

PubMed1962

Separation of acid phosphatase from tributyrinase and plasma clotting activities in partially purified staphylocoagulase.

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Acid Phosphatase↗

PubMed1962

Enzymatic activities associated with clotting of fibrinogen by staphylocoagulase and coagulase-reacting factor and their inhibition by disopropylfluophosphate.

Drummond, Margaret C. (Emory University, Atlanta, Ga.) and Morris Tager. Enzymatic activities associated with clotting of fibrinogen by staphylocoagulase and coagulase-reacting factor and their inhibition by diisopropylfluorophosphate. J. Bacteriol. 83:975-980. 1962.-The chemical mechanism of fibrinogen clotting by staphylocoagulase and its plasma factor (CRF) involves a preliminary stage of proteolysis, analogous to that found in thrombin-catalyzed fibrinogen clotting. Coagulase-CRF also exhibits N-alpha-toluene-p-sulfonyl-l-arginine methyl esterase activity in addition to its fibrinogen-clotting and proteolytic activities. These enzymatic activities have been further studied by their responses to certain enzyme inhibitors, and from the standpoint of their possible interrelationships.

Arginine↗

PubMed1959