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[22] Plasminogen and plasmin

descriptionPublicationkeyboard_double_arrow_right Part of book or chapter of book , Article 01 Jan 1976Publisher:Elsevier BV

Authors: Kenneth C. Robbins; Louis Summaria;

doi: 10.1016/s0076-6879(76)45025-5

pmid: 138064

[22] Plasminogen and plasmin

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Abstract

Publisher Summary Plasmin is a serine protase with trypsin-like specificity. It cleaves or hydrolyzes proteins and peptides at arginyl and lysyl peptide bonds, and basic amino acid esters, and amides. Plasmin appears to have a preference for lysyl bonds in both protein and ester substrates. Assay methods for plasminogen and plasmin have been devised using both casein (caseinolytic) and fbrin (fibrinolytic) substrates; in the caseinolytic assay, the release of trichloroacetic acid, or perchloric acid, soluble peptides arc measured, and in the fibrinolytic assay, the time of dissolution of the fibrin clot is determined. This chapter describes specific active-site titration methods developed to determine the amount of enzyme in solution. Specific antibody and protein inhibitor assays have also been described. A method for the determination of human plasminogen and plasmin based on the interaction between the zymogen, or enzyme, and streptokinase has been described.

Keywords

Binding Sites, Isoflurophate, Macromolecular Substances, Plasminogen, Tosyllysine Chloromethyl Ketone, Thromboplastin, Enzyme Activation, Isoenzymes, Terminology as Topic, Methods, Serine, Animals, Humans, Histidine, Amino Acid Sequence, Fibrinolysin, Rabbits, Amino Acids

Impact byBIP!

	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	109
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	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 1%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 10%