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Biomedical subjects

J M Becker

Publications and source records attributed to J M Becker.

At least 253 records · Page 14Linked to original sources
PubMed1974

Stereospecificity of tripeptide utilization in a methionine auxotroph of Escherichia coli K-12.

The stereospecificity of peptide utilization in Escherichia coli K-12 4212, a methionine auxotroph, was investigated using diastereomers of trimethionine and trimethionine methyl ester. Of the eight stereoisomers examined, only l-Met-l-Met-l-Met, l-Met-l-Met-d-Met, and d-Met-l-Met-l-Met and the corresponding methyl esters serve as growth substrates. Triornithine-resistant mutants of strain 4212 were isolated which failed to transport d-Met-l-Met-l-Met. These results provide evidence that an oligopeptide containing a d residue at its amine terminus can enter E. coli by the oligopeptide transport system.

Cell-Free System↗
PubMed1971

Irreversible inhibition of biotin transport in yeast by biotinyl-p-nitrophenyl ester.

Biotinyl-p-nitrophenyl ester (BNP), an active-ester derivative of biotin, irreversibly inactivates biotin transport in the yeast Saccharomyces cerevisiae. Transport inactivation is progressive with time and occurs at concentrations of the ester as low as 10(-7) M. In the presence of sodium azide, a reagent known to block biotin accumulation in yeast, the derivative is still effective. The specificity of inactivation by the ester is revealed by the following findings: (a) Biotinyl-p-nitroanilide and acetyl-p-nitrophenyl ester do not affect biotin transport; (b) the nitrophenyl ester does not affect the transport of lysine and aspartic acid, or that of L-sorbose; (c) inactivation of biotin transport by the ester is partially prevented when the cells are incubated with it in the presence of relatively high concentrations of biotin.

Amino Acids↗
PubMedDate not supplied

Conformational studies of nikkomycin X in aqueous solution.

Nikkomycin X is a peptidyl-nucleoside antibiotic that inhibits chitin synthesis in fungi. Information on its conformation in aqueous solution was obtained from pH titration studies in which the nmr shifts of exchangeable and nonexchangeable protons were monitored. These studies and nuclear Overhauser effects support an unfolded or conformationally flexible structure for the antibiotic, and the syn and anti conformations of the nucleoside moiety were found to coexist. The conformation of the ribose ring was determined using a two-state model; a slight shift from type N to type S conformers occurred as the pH was raised from 1 to 6.

Aminoglycosides↗