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Plasmin

  • Chapter
Fibrinolytics and Antifibrinolytics

Abstract

Plasminogen, the zymogen precursor of plasmin, can be separated from mammalian plasmas, serums, and enriched plasma fractions (e.g., fractions III and III2,3) by an affinity chromatography method with either L-lysine-substituted-Sepharose (Deutsch and Mertz, 1970; Robbins and Summaria, 1976) or Polyacrylamide (Rickli and Cuendet, 1971), and either p-aminobenzamidine-substituted Sepharose (Holleman et al., 1975) or n-butyl p-aminobenzoate-substituted Sepharose (Zolton and Mertz, 1972). Heparin influences the affinity of human plasminogen for L-lysine-substituted Sepharose, and inhibits its elution by ε-aminocaproic acid (Hatton and Regoeczi, 1976). These zymogen preparation can also be prepared by ion-exchange and gel-filtration methods (Robbins and Summaria, 1970; Wallén and Wiman, 1970), and the affinity chromatography preparations can be further purified to homogeneity by both ion-exchange chromatography and gel-filtration methods (Robbins et al., 1975). Human native (Glu-plasminogen), and partially degraded (Lys-plasminogen) zymogens, have been prepared and characterized; the hydrodynamic properties of these forms are summarized in Table 1.

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  1. K. C. Robbins
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  1. Institut für Pharmakologie und Toxikologie, Medizinische Akademie Erfurt, Nordhäuser Straße 74, Erfurt, German Democratic Republic

    F. Markwardt

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Robbins, K.C. (1978). Plasmin. In: Markwardt, F. (eds) Fibrinolytics and Antifibrinolytics. Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology, vol 46. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66863-0_11

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  • DOI: https://doi.org/10.1007/978-3-642-66863-0_11

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