PMID:3897225
| Citation |
Guyer, CA, Morgan, DG, Osheroff, N and Staros, JV (1985) Purification and characterization of a periplasmic oligopeptide binding protein from Escherichia coli. J. Biol. Chem. 260:10812-8 |
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| Abstract |
We have purified and characterized an oligopeptide binding protein released from the periplasm of Escherichia coli W by mild osmotic shock. The purified protein was greater than 97% homogeneous as determined by either sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Mr = 60,000) or isoelectric focusing (pI = 5.95). The binding protein has a Stokes radius of 30 A and a sedimentation coefficient (s(0)20,w) of 4.6 S. Based on these hydrodynamic studies, the native protein has a molecular weight of 56,000. The tripeptide, Ala-Phe-[3H]Gly, which is transported via the shock-sensitive sensitive oligopeptide permease, binds to the purified protein in dilute solution with a Kd of 0.1 microM and a stoichiometry of approximately 1 to 1. Results from this study support the hypothesis that this periplasmic oligopeptide binding protein functions in the initial recognition of peptide substrates for the oligopeptide permease system. |
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| Keywords |
Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism; Chromatography, DEAE-Cellulose; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Lipoproteins; Molecular Weight; Oligopeptides/metabolism; Protein Conformation |
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