Isolation and Characterization of Microbial Immunoglobulin A Protease.
Annual rept. 1 Jan-31 Dec 74,
NEW ENGLAND MEDICAL CENTER HOSPITAL BOSTON MASS
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The annual report summarizes research on a contract to isolate and characterize proteolytic enzymes from bacteria. The work has to principally involved IgA protease, a proteolytic enzyme derived from normally occurring gastrointestinal bacteria. This enzyme is highly specific in that it proteolytically cleaves only human IgA immunoglobulin to yield Fcalpha and Fabalpha fragments. In the past year, the authors have identified an organism suitable for producing this enzyme in high yield, determined proper growth characteristics for enzyme production, have worked out a method for preliminary purification, and have characterized the specific peptide bond cleaved by this enzyme in IgA proteins. An assay procedure has been set up for the enzyme, a problem made difficult by the fact that the enzyme only cleaves IgA and does not work on smaller substrates. Finally, a similar enzyme has been identified in broth culture filtrates of Neisseria gonorrhoeae and N. meningitides.
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