This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Griebel, R. J. Articles by Merrick, J. M. Search for Related Content PubMed PubMed Citation Articles by Griebel, R. J. Articles by Merrick, J. M.

Metabolism of Poly-ß-Hydroxybutyrate: Effect of Mild Alkaline Extraction on Native Poly-ß-Hydroxybutyrate Granules¹

^a Department of Biology, Syracuse University, Syracuse, New York 13210
^b Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214

ABSTRACT

Mild alkaline extraction of native poly-ß-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). A-I but not A-II can be recombined with extracted granules to give rise to PHB synthetase activity. Extracted granules no longer require pretreatment with activator or trypsin but are directly susceptible to hydrolysis by Rhodospirillum rubrum depolymerase. Addition of A-II or A-I prevents the direct hydrolysis by depolymerase. The inhibition is reversed by activator or trypsin. We conclude that native granules are associated with a protein inhibitor which prevents the hydrolysis of PHB by depolymerase unless the protein is destroyed by trypsin, removed by alkaline extraction, or modified by activator.

² Present address: Veterans Administration Hospital, Research Service (151), Bedford, Mass. 01730.

¹ Taken in part from a dissertation submitted by R. J. Griebel to Syracuse University in partial fulfillment of the requirements for the Ph.D. degree.

This article has been cited by other articles:

• Handrick, R., Reinhardt, S., Kimmig, P., Jendrossek, D. (2004). The "Intracellular" Poly(3-Hydroxybutyrate) (PHB) Depolymerase of Rhodospirillum rubrum Is a Periplasm-Located Protein with Specificity for Native PHB and with Structural Similarity to Extracellular PHB Depolymerases. J. Bacteriol. 186: 7243-7253 [Abstract] [Full Text]  
• McCool, G. J., Cannon, M. C. (2001). PhaC and PhaR Are Required for Polyhydroxyalkanoic Acid Synthase Activity in Bacillus megaterium. J. Bacteriol. 183: 4235-4243 [Abstract] [Full Text]