Purification and Characterization of a High-Mr Proteinase Inhibitor of Pro-phenol Oxidase Activation from Crayfish Plasma

Overview

Journal Biochem J

Specialty Biochemistry

Date 1987 Nov 15

PMID 3124809

Citations 12

Authors

H G Hergenhahn

A Aspan

K Soderhall

Affiliations

Soon will be listed here.

Abstract

Crayfish plasma was found to contain a proteinase inhibitor, which was purified to apparent homogeneity by acid precipitation, affinity chromatography on concanavalin A-Sepharose and hydrophobic-interaction chromatography. The inhibitor is a monomeric protein with an Mr of about 155,000 and a pI in the range 4.6-4.8. It is heat-stable and tolerant to low pH. It inhibits the serine proteinases trypsin and chymotrypsin, but not thrombin or subtilisin. Furthermore, it is efficient in decreasing the activity of a proteinase from crayfish haemolymph that is involved in the activation cascade of pro-phenol oxidase and can also block pro-phenol oxidase activation by this serine proteinase. This cascade is believed to play a central role in the recognition mechanism of non-self material in crustaceans and insects. The data presented give some evidence that the new proteinase inhibitor is involved in the regulation of this system.

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