Synthesis of a selenomethionine peptide and a preliminary study of transport into Escherichia coli monitored by high-performance liquid chromatography.
The tripeptide Gly-SeMet-Gly has been synthesized by a combination of solution and solid-phase methods. Increase in weight of the resin was very nearly theoretical, and purification was straightforward. Its absorption was compared to that of the corresponding peptide, Gly-Met-Gly, in E. coli using HPLC ion-exchange separation and fluorometric determination of the disappearance of peptides in the culture medium and the appearance of methionine and selenomethionine in the same culture medium. As E. coli are not known to possess extracellular peptidases, and in fact have been shown to possess transport systems for peptides, this absorption is interpreted as transport of the peptide through the cell wall and membrane into the cytoplasm, endohydrolysis of the peptide, and efflux of the peptides' amino acids. Uptake of both peptides was approximately equal, but was slowed when both peptides were present simultaneously.
Kochansky
J P
JP
Insect Neurobiology and Hormone Laboratory, US Department of Agriculture, Beltsville, Maryland, USA.
Tschursin
E
E
Lusby
W R
WR
Lacroix
D
D
Wolf
W R
WR
D000595:Amino Acid Sequence; D001692:Biological Transport / Q000502:physiology; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism*; D012645:Selenomethionine / Q000138:chemical synthesis* / Q000378:metabolism
D010455:Peptides; D012645:Selenomethionine