Extracellular enzyme secretion by Pseudomonas lemoignei.

The ability of succinate to repress the secretion of Pseudomonas lemoignei poly-beta-hydroxybutyrate depolymerase was a function of pH. Repression only occurred when the pH of the medium was 7.0 or less.

Metabolism of poly- -hydroxybutyrate: effect of mild alkaline extraction on native poly- -hydroxybutyrate granules.

Mild alkaline extraction of native poly-beta-hydroxybutyrate (PHB) granules results in the solubilization of a protein fraction. Both the solubilized protein fraction and the extracted granules are essentially devoid of PHB synthetase activity unless recombined. The protein fraction has been separated by chromatography into two components (A-I and A-II).

Identification of propionate as an endogenous CO2 acceptor in Rhodospirillum rubrum and properties of purified propionyl-coenzyme A carboxylase.

A heat-stable endogenous CO(2) acceptor has been found in extracts of Rhodospirillum rubrum grown photoheterotrophically on acetate. Evidence is presented which suggests that this factor is propionic acid. Thus, paper and gas chromatographic analyses have indicated that propionic acid is present in boiled extracts prepared from R.

Effect of polymyxin B, tyrocidine, gramicidin D, and other antibiotics on the enzymatic hydrolysis of poly-beta-hydroxybutyrate.

Merrick, J. M. (State University of New York, Buffalo).

MORPHOLOGICAL CHANGES IN POLY-BETA-HYDROXYBUTYRATE GRANULES ASSOCIATED WITH DECREASED SUSCEPTIBILITY TO ENZYMATIC HYDROLYSIS.

Merrick, J. M. (State University of New York, Buffalo), D.

DEPOLYMERIZATION OF POLY-BETA-HYDROXYBUTYRATE BY INTRACELLULAR ENZYME SYSTEM.

Merrick, J. M. (State University of New York, Buffalo), and M.