Isolation and Characterization of Microbial Immunoglobulin A Protease.

Abstract

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 Fc(alpha) and Fab(alpha) 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.

Document Details

Document Type
Technical Report
Publication Date
Mar 07, 1975
Accession Number
ADA009569

Entities

People

  • Andrew G. Plaut

Tags

DTIC Thesaurus Topics

  • Bacteria
  • Contracts
  • Immunoglobulins
  • Microorganisms
  • Production
  • Prokaryotes
  • Proteins
  • Substrates

Fields of Study

  • Biology

Readers

  • Microbial Pathology
  • Molecular and Cellular Biochemistry

Technology Areas

  • Biotechnology