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Biomedical subjects

J L Strominger

Publications and source records attributed to J L Strominger.

At least 613 records · Page 34Linked to original sources
PubMed1969

Structure of the peptidoglycan of bacterial spores: occurrence of the lactam of muramic acid.

Six major oligosaccharides were released from the peptidoglycan of spores of Bacillus subtilis by lysozyme treatment. They were isolated and characterized as a disaccharide, tetrasaccharide, and hexasaccharide composed of equal amounts of muramic acid and glucosamine and containing two, three, and four acetyl groups, respectively. Three of the compounds were substituted by a single L-alanine residue, and the other three by a single tetrapeptide substituent on the acetylmuramic acid residue at the reducing end of each compound. The other muramic acid residue in the tetrasaccharides (and two of the three in the hexasaccharides) were shown to be present as muramic lactams, a sugar not previously found in nature and, hence, a unique spore constituent. Other features of the structure of spore peptidoglycan are discussed.

Bacillus subtilis↗
PubMed1969

Specificity of a bacteriolytic enzyme from Pseudomonas aeruginosa.

A bacteriolytic enzyme isolated from shake-flask cultures of Pseudomonas aeruginosa and capable of lysing cells of Staphylococcus aureus was purified approximately 500-fold by passage through diethylaminoethyl cellulose and chromatography on carboxymethyl-cellulose. The purified enzyme was shown to act as an endopeptidase, cleaving the pentaglycine cross-bridges of the cell wall peptidoglycan at d-alanyl-glycine and glycyl-glycine linkages with the release of di-, tri-, and tetraglycine fragments. Release of NH(2)-alanine indicated weak N-acetylmuramyl-l-alanine amidase activity, but most of the residual peptide remained attached to the glycan. No hydrolysis of the glycan occurred. The lytic spectrum of the enzyme toward a variety of other cell walls of known peptidoglycan composition indicated relatively high specificity for peptidoglycans with polyglycine bridges.

Aminohydrolases↗