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. 1967 Feb;102(2):554–563. doi: 10.1042/bj1020554

Studies on the proteolytic activity of γ-globulin preparations

B Robert 1, R S Bockman 1
PMCID: PMC1270280  PMID: 4166042

Abstract

1. The proteolytic activities of several γ-globulin preparations were tested. These included sulphate-precipitated human and bovine preparations and human and bovine Cohn fraction II preparations as well as purified γ-globulin preparations. Up to 14mg. of diffusible peptides and glycopeptides/g. of γ-globulin was liberated after dialysis and up to 10mg. of peptides/g. after incubation and trichloroacetic acid precipitation, as products of the degradation process in incubated γ-globulin. 2. ∈-Aminohexanoic acid and p-chloromercuribenzoic acid, as well as heating at 60° for 40min., were shown to inhibit strongly these proteolytic activities. Streptokinase was shown to activate strongly the proteolytic activity of all the human preparations (sulphate-precipitated, Cohn fraction II, and purified γ-globulin). 3. Two distinct pH optima were shown for human and bovine γ-globulin preparations: one at pH8, the other at pH3·8 (the latter activity could be demonstrated only in the presence of cysteine). 4. Both 131I-labelled human Cohn fraction II and bovine fibrinogen were attacked by a sulphate-precipitated preparation of γ-globulin. Of the synthetic substrates tested toluene-p-sulphonyl-l-arginine methyl ester was hydrolysed by both the sulphate-precipitated and Cohn fraction II preparations, as was benzoyl-l-arginine amide at pH5, but only in the presence of cysteine. 5. These data are interpreted to indicate that at least two enzymes are present in γ-globulin preparations, one being similar to the plasmin system, the other similar to cathepsin B.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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