1965
DOI: 10.1111/j.1749-6632.1965.tb11632.x
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Staphylocoagulase *

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Cited by 29 publications
(6 citation statements)
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“…These globular domains are connected by long triple-helical structures. Coa·prothrombin complexes, which convert human fibrinogen to the self-polymerizing fibrin, are not targeted by circulating thrombin inhibitors [19], allowing coagulase to bypass the physiological regulatory steps of blood coagulation pathways [21].…”
Section: Introductionmentioning
confidence: 99%
“…These globular domains are connected by long triple-helical structures. Coa·prothrombin complexes, which convert human fibrinogen to the self-polymerizing fibrin, are not targeted by circulating thrombin inhibitors [19], allowing coagulase to bypass the physiological regulatory steps of blood coagulation pathways [21].…”
Section: Introductionmentioning
confidence: 99%
“…Presumptive MRSA were further screened for coagulase and thermonuclease production. A part of colony was emulsified in normal saline then mixed with rabbit plasma; clumping indicated positive result [ 17 ]. Colonies grown on BHI agar were further incubated for 2 h at 60°C and overlaid with thermonuclease agar and further incubated at 37°C till the development of pink zone around the positive control [ 18 ].…”
Section: Methodsmentioning
confidence: 99%
“…SC nonproteolytically activates the blood coagulation zymogen, prothrombin (ProT) through interactions localized to the N-terminal 324 residues, and the SC-(1-325)⅐(pro)thrombin catalytic complex recognizes and cleaves fibrinogen (Fbg) as a specific substrate (2)(3)(4). The C-terminal region of SC contains five to eight 27-residue repeat sequences that mediate distinctly different Fbg binding interactions (5).…”
Section: Staphylocoagulase (Sc)mentioning
confidence: 99%