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J Bacteriol. 1968 December; 96(6): 1969-1976
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Characterization of a Human Serum Inhibitor of Clostridium histolyticum Proteinase(s)1

Alma Luzzati2, Marvin B. Goldlust3 and Lawrence Levine

a Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02154

ABSTRACT

Normal animal sera inhibit at least one Clostridium histolyticum proteinase. An assay procedure based on immune hemolysis was developed for the estimation of this inhibition. This inhibitory activity occurs in various levels in the sera of different animal species. The highest titers have been obtained with rat sera. The inhibitory activity from human serum was isolated and purified 16- to 27-fold by Sephadex G-200 gel filtration and diethylaminoethyl cellulose or hydroxylapatite chromatography. The properties of the human serum inhibitor of the clostridial proteinase were compared with a trypsin inhibiting factor found in the partially purified preparations. Identical behavior of the two inhibitory factors was observed when measured by heat inactivation, ß-mercaptoethanol sensitivity, pH stability, and sucrose gradient centrifugation. The inhibitory factor has an approximate sedimentation coefficient (S20,w) of 17. Goat anti–{alpha}-2-macroglobulin specifically precipitated the clostridial proteinase inhibitor from a partially purified preparation.

FOOTNOTES

2 Present address: Institute of Medical Genetics, University of Turin, Turin, Italy.

3 Present address: Department of Microbiology, The Johns Hopkins University, School of Medicine, Baltimore, Md. 21205.

1 Publication no. 607 of the Graduate Department of Biochemistry, Brandeis University, Waltham, Mass.

J Bacteriol. 1968 December; 96(6): 1969-1976
Copyright © 1968 American Society for Microbiology. All Rights Reserved.





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