[Retroaldol cleavage of the glyopeptide antibiotic ristomycin A during alkaline inactivation].

The chemical and physicochemical characteristics of one of the two inactive components, i.e. the reduced product of alkaline inactivation (PAH-II) of ristomycin. A were studied. The components formed on the antibiotic incubation in mild alkaline media: 0.05 M NaOH, 37 degrees C, 1.5-2 hours. It was shown that the retroaldol cleavage of the C alpha-C beta bond of the phenol serine fragment of the trinuclear dideschlorvancomycinic acid G at the aglycone N-end was one of the causes of ristomycin A rapid inactivation under such conditions.