Subject(s)
Consent Forms , Forms and Records Control/legislation & jurisprudence , Hospital Administration/legislation & jurisprudence , Informed Consent/legislation & jurisprudence , Adolescent , Disclosure , Humans , Liability, Legal , Mental Competency/legislation & jurisprudence , Minors , Ontario , Parental Consent , Physician-Patient Relations , Planning Techniques , Risk Assessment , Treatment RefusalABSTRACT
Countercurrent distribution is capable of resolving mixtures of closely related prodigiosene pigments. Syntrophic pigment produced by several pairs of Serratia marcescens color mutants was identified as prodigiosin (2-methyl-3-amyl-6-methoxyprodigiosene) by countercurrent distribution, soda lime pyrolysis, and other techniques. The metabolic block of mutant strain H-462, derived from parent strain HY, was located between the blocks of mutant strains OF and WF, both derived from parent strain Nima.
Subject(s)
Prodigiosin/analysis , Serratia marcescens/analysis , Bacteriological Techniques , Chromatography, Thin Layer , Colorimetry , Culture Media , Genetics, Microbial , Hot Temperature , Mutation , Prodigiosin/biosynthesis , Prodigiosin/isolation & purification , Serratia marcescens/metabolismSubject(s)
Anti-Bacterial Agents/biosynthesis , Pigments, Biological/biosynthesis , Pyrroles/biosynthesis , Serratia marcescens/metabolism , Carbon Isotopes , Chemical Phenomena , Chemistry , Genetics, Microbial , Glycine/metabolism , Maleimides/chemical synthesis , Methionine/metabolism , Mutation , Oxidation-Reduction , Prodigiosin/biosynthesis , Proline/metabolism , Serratia marcescens/growth & developmentSubject(s)
Anti-Bacterial Agents/chemical synthesis , Pigments, Biological/chemical synthesis , Pyrroles/chemical synthesis , Serratia marcescens/metabolism , Anti-Bacterial Agents/biosynthesis , Pigments, Biological/biosynthesis , Prodigiosin/chemical synthesis , Pyrroles/biosynthesis , Spectrum AnalysisABSTRACT
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.