A Novel Immunological Technique for Detection of  Gramicidin (S) Producing Bacteria

The development of a quantitative immunological technique using polyvalent antiserum permits a more logical approach to the fractionation of complex protein mixtures. In this study whole serum was separated by conventional gel filtration and the fractions obtained were analysed. This demonstrates over 60 immunologically distinct serum proteins. Because the current terminology is inadequate to describe this number of proteins, a temporary numerical nomenclature has been used.

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The demonstration of rupture of cell surfaces by an immunological technique

Experimental Cell Research ◽

10.1016/0014-4827(63)90304-5 ◽

1963 ◽

Vol 30 (2) ◽

pp. 331-338 ◽

Cited By ~ 47

Author(s):

L. Weiss ◽

R.R.A. Coombs

Keyword(s):

Cell Surfaces ◽

Immunological Technique

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The synthesis of peptides related to gramicidin S and the significance of optical configuration in antibiotic peptides. 1. Tripeptides

Biochemical Journal ◽

10.1042/bj0460196 ◽

1950 ◽

Vol 46 (2) ◽

pp. 196-199 ◽

Cited By ~ 22

Author(s):

J. I. Harris ◽

T. S. Work

Keyword(s):

Gramicidin S ◽

Optical Configuration ◽

Antibiotic Peptides

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Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50

Biochemical Journal ◽

10.1042/bj1790333 ◽

1979 ◽

Vol 179 (2) ◽

pp. 333-339 ◽

Cited By ~ 13

Author(s):

A Y Strongin ◽

D I Gorodetsky ◽

I A Kuznetsova ◽

V V Yanonis ◽

Z T Abramov ◽

...

Keyword(s):

Bacillus Subtilis ◽

Serine Proteinase ◽

Subtilis Strain ◽

Bacterial Strains ◽

Terminal Sequence ◽

Gramicidin S ◽

Intracellular Enzymes ◽

Sepharose 4B ◽

Homologous Enzyme ◽

Strict Selection

Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the amino acid composition and the 19 residues of the N-terminal sequence of the enzyme are reported. The isolated proteinase was closely related to, but not completely identical with, the intracellular serine proteinase of B. subtilis A-50. The divergence between these two intracellular enzymes was less than that between the corresponding extracellular serine proteinases (subtilisins) of types Carlsberg and BPN′!, produced by these bacterial strains. This may be connected with the more strict selection constraints imposed in intracellular enzymes during evolution.

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