Purification and Characterization of the Outer Membrane Lipo Protein from an Escherichia-Coli Mutant Altered in the Signal Sequence of Pro Lipo Protein

Lin, J. J. C., Kanazawa, H., Wu, H. C. (1980) Purification and Characterization of the Outer Membrane Lipo Protein from an Escherichia-Coli Mutant Altered in the Signal Sequence of Pro Lipo Protein. Journal of Biological Chemistry, 255 (3). pp. 1160-1163.

URL: https://pubmed.ncbi.nlm.nih.gov/6985905

Abstract

Lipoprotein was purified to homogeneity from an E. coli strain carrying a mutation in the structural gene for murein lipoprotein (mlpA). The primary structure of the mutant lipoprotein was determined. The mutant lipoprotein corresponds to an uncleaved prolipoprotein with a single amino acid substitution of glycine by aspartic acid at the 14th residue.

Item Type: Paper
Subjects: organism description > bacteria > escherichia coli
CSHL Authors:
Communities: Cold Spring Harbor Laboratory of Quantitative Biology
Depositing User: Elizabeth Pessala
Date: 1980
Date Deposited: 07 May 2020 19:45
Last Modified: 07 May 2020 19:45
URI: https://repository.cshl.edu/id/eprint/39320

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