Thrombinwirkung und Fibrinolyse in gereinigten Gerinnungs-systemen

Hudemann, Sylvia

doi:10.1007/bf01510777

Cited by 16 publications

(2 citation statements)

References 56 publications

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“…Of paramount importance is the question whether chymotrypsinogen was activated by the thrombin, or by contaminants of trypsin, of trypsinlike enzymes, of other proteases or arginyl esterases, all of which have been described in blood (Gullick, 1963;Hudemann, 1940;Brakman et al, 1964;Mehl et al, 1964;Floch and Groisser, 1960), as well as in commercial and partially purified thrombin preparations (Hudemann, 1940;Brakman et al, 1964). Every effort has been made to resolve this question by the use of appropriate differentiating inhibitors and experimental conditions.…”

Section: Discussionmentioning

confidence: 99%

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Engel¹,

Alexander²

1966

Biochemistry

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Earlier demonstration that thrombin resembles trypsin in the ability to convert trypsinogen and plasminogen to their respective proteases prompted investigation of its effect on chymotrypsinogen A. Purified thrombin added to the zymogen induced rapid and progressive appearance of esterolytic activity toward acetyltyrosyl ethyl ester. The addition of indole to the zymogen-thrombin mixture after interaction had proceeded obviated esterolysis, indicating that the evolved activity was due to chymotrypsin. Elaboration of the active enzyme from its precursor appeared to take place in accord with enzyme kinetics, the thrombin functioning enzymatically on the zymogen. That this was not due to a possible trypsin contaminant of the thrombin was demonstrated with appropriate inhibitors, by procedures known to block thrombic action, and by separation of certain known contaminants, which T hrombin resembles trypsin in many enzymatic properties (Sherry and Troll, 1954; MiUer and Van Vunakis, 1956;Gladner and Laki, 1956; Laki et al., 1958;Martin et al., 1959;Ronwin, 1960;Laki and Gladner, 1964;Sherry et al., 1965; KCzdy et al., 1965), including the ability to activate trypsinogen and plasminogen (Engel et al., 1966). Since cleavage of the ester and peptide bonds of many synthetic substrates (Ehrenpreis et al., 1957;Lorand et al., 1962;Elmore and Curragh, 1963; Baird ef al., 1965) and proteins1 are catalyzed by both enzymes, and since trypsin activates chymotrypsinogen, the question whether thrombin can similarly activate this zymogen was explored.

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Section: Discussionmentioning

confidence: 99%

Activation of Chymotrypsinogen-A by Thrombin Preparations^*

Engel¹,

Alexander²

1966

Biochemistry

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“…Hudemaiin (7) first demonstrated that a fibrinolytic component i11 thrombin preparations could be separated from the thrombin. She used fractional precipitation with ammonium sulfate.…”

Section: Discussionmentioning

confidence: 99%

Fibrinolytic Activity of Thrombin Preparations

Brakman¹,

Klug²,

Astrup³

1964

Thromb Haemost

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SummarySome thrombin samples have a slight unspecific protease activity probably caused by contaminating plasmin. All investigated samples were fibrinolytically active. This activity was caused by an activator of plasminogen. Fibrinolytic activity was apparently produced by two components of the thrombin preparations. One of these components was a contaminant with fibrinolytic activity but with no thrombin activity. This component could be separated from the thrombin by simple chemical procedures. The other fibrinolytic component appeared to be the thrombin molecule per se. It was not fibrinolytically active when used in the low concentrations required for clotting of fibrinogen, but in high concentrations, assayed on the fibrin plate, it activated plasminogen. In the accurate assay of fibrinolytic agents it is necessary to use preparations of thrombin from which the contaminating fibrinolytic agent has been removed.

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