Isolation, purification, and partial characterization of Brucella abortus matrix protein.

Infection and Immunity
I Moriyon, D T Berman

Abstract

Peptidoglycan sacculi with peptidoglycan-associated proteins were prepared from cell envelopes of Brucella abortus by extraction with sodium dodecyl sulfate (SDS) at 50 degrees C. On extraction of these preparations with SDS at 100 degrees C, a protein was obtained whose removal from peptidoglycan was confirmed by electron microscopy. Incubation of the 50 degrees C SDS-extracted cell envelopes with 50 mM MgCl2 in SDS-2-beta-mercaptoethanol at 37 degrees C also extracted the protein, along with lipopolysaccharide. At temperatures below 60 degrees C, the protein did not bind SDS strongly and had an apparent molecular weight greater than 92,000 in SDS-polyacrylamide gel electrophoresis. At higher temperatures, SDS bound strongly, and the apparent molecular weight was 38,000. Urea at 5 M did not alter the electrophoretic mobility of this 38,000-molecular-weight form. Immunoelectrophoresis in detergents with antisera to cell envelopes, carbohydrate staining of SDS-polyacrylamide gels, and production of anti-lipopolysaccharide antibodies by mice immunized with the purified protein indicated that lipopolysaccharide was present in free and protein-bound forms. Sequential gel filtration in SDS-EDTA and SDS-NaCl removed most lipopolysacc...Continue Reading

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Citations

Nov 19, 2015·Frontiers in Microbiology·Shivani GoolabMichael C Crampton
Feb 1, 1990·Infection and Immunity·J I Riezu-BojR Díaz
Jan 1, 1987·Annales De L'Institut Pasteur. Microbiology·D T Berman, R S Kurtz
Jan 1, 1987·Annales De L'Institut Pasteur. Microbiology·A J Winter
Jan 1, 1987·Annales De L'Institut Pasteur. Microbiology·I MoriyónR Díaz
Nov 1, 1987·Journal of Clinical Microbiology·M AfzalP G Squire

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