TY - JOUR
T1 - Isolation of glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis
AU - Kleene, S. J.
AU - Toews, M. L.
AU - Adler, J.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1977
Y1 - 1977
N2 - Glutamic acid 5-methyl ester was isolated from an E. coli protein involved in chemotaxis. The bacteria were first incubated with [methyl-3H] methionine under conditions which are known to result in methylation of the protein. The protein, isolated by gel electrophoresis, was then digested by successive treatment with three proteolytic enzymes. One of the products was [methyl-3H] glutamic acid 5-methyl ester, identified by comparison with an authentic sample in the following studies: chromatography on an automatic amino acid analyzer, chromatography on paper in two solvent systems, chromatography on paper of the N-acetyl derivatives, and stability of the ester bond to various pH conditions. No aspartic acid 4-methyl ester was found in the enzymatic digest. Treatment of the methylated protein with alkali released the radioactivity as [3H] methanol, which was identified by gas chromatography and by preparation of the 3,5-dinitrobenzoate.
AB - Glutamic acid 5-methyl ester was isolated from an E. coli protein involved in chemotaxis. The bacteria were first incubated with [methyl-3H] methionine under conditions which are known to result in methylation of the protein. The protein, isolated by gel electrophoresis, was then digested by successive treatment with three proteolytic enzymes. One of the products was [methyl-3H] glutamic acid 5-methyl ester, identified by comparison with an authentic sample in the following studies: chromatography on an automatic amino acid analyzer, chromatography on paper in two solvent systems, chromatography on paper of the N-acetyl derivatives, and stability of the ester bond to various pH conditions. No aspartic acid 4-methyl ester was found in the enzymatic digest. Treatment of the methylated protein with alkali released the radioactivity as [3H] methanol, which was identified by gas chromatography and by preparation of the 3,5-dinitrobenzoate.
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M3 - Article
C2 - 16888
AN - SCOPUS:0017392255
VL - 252
SP - 3214
EP - 3218
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 10
ER -