ISSN:
1618-2650
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Description / Table of Contents:
Zusammenfassung Die Bestimmung von Inhibitoren für die Proteinasen Trypsin, Chymotrypsin, Plasmin, Thrombin und für Kallikreine in Gewebsextrakten und Körperflüssigkeiten wird diskutiert. Mit Hilfe wasserunlöslicher Proteinaseharze lassen sich Inhibitoren dieser Enzyme auf einfache und spezifische Weise aus den Extrakten isolieren. Die Aminosäurezusammensetzung der aus Pankreas von Rind, Schwein und Hund isolierten spezifischen Trypsininhibitoren wird angegeben. In ähnlicher Weise eignen sich auch wasserunlösliche Inhibitorharze zur Isolierung von Enzymen und zur einfachen Trennung von Proteinasegemischen.
Notes:
Abstract Estimation procedures for inhibitors of the proteinases trypsin, chymotrypsin, plasmin (fibrinolysin), thrombin and kallikreins in extracts of organs and body fluids are discussed. Best results are obtained with synthetic substrates, e.g. N-benzoyl-arginine-p-nitroanilide (for trypsin), N-(3-carboxypropionyl)-l-phenylalanine-p-nitroanilide (for chymotrypsin) and N-benzoyl-argininethylester (for plasmin, thrombin, kallikreins). Water-insoluble resins (copolymers of ethylene and maleic acid) of proteinases are very suitable for the specific isolation of proteinase inhibitors from crude extracts of plants and organs. Inhibitors of relative low molecular weight (near 6,000) are bound in neutral buffer solutions in complex form to the proteinase, which is covalently fixed to the polyanionic carrier. Inhibitors of high molecular weights and low isoelectric points (below 6) are bound only to the fixed proteinase if the polyanionic character of the resin is “neutralized”. Thus we succeeded in isolating, e.g., inhibitors from soyabeans and egg white. The inhibitors are dissociated from the proteinase resins in acidic salt solutions and in urea or guanidine solutions. Water-insoluble resins of the trypsin-kallikrein inhibitor from beef organs are suitable for the isolation of trypsin, chymotrypsin and kallikreins in a similar manner.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00530725
