Affiliation:
1. National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, U.S. Public Health Service, Bethesda, Maryland
Abstract
Warren, Leonard
(National Institute of Arthritis and Metabolic Diseases, Bethesda, Md.)
and C. W. Spearing
. Sialidase (neuraminidase) of
Corynebacterium diphtheriae
. J. Bacteriol.
86:
950–955. 1963.—The characteristics of a sialidase produced by
Corynebacterium diphtheriae
were studied. The enzyme was partially purified from preparations of diphtheria toxin on a column of Sephadex G-75. By this means the lethal factor of diphtheria toxin was separated, in part, from the sialidase activity. There appeared to be a close immunological relationship between the sialidases of
C. diphtheriae
and clostridia, since a preparation of diphtheria antitoxin was as effective an inhibitor of diphtheria sialidase as of the sialidase of three species of clostridia. Conversely, antitoxin to clostridia inhibited diphtheria sialidase. Diphtheria antitoxin was essentially inactive toward influenza virus sialidase, and was completely inactive against purified sialidase of
Vibrio cholerae
. Removal of sialic acid from the proteins in a preparation of diphtheria antitoxin did not alter the inhibitory activity of the antitoxin against diphtheria sialidase. The enzyme operated optimally at pH 5.5 and did not require calcium ions for activity. The substrate specificity of diphtheria sialidase appears to be the same as that of other previously described sialidases.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
41 articles.
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