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. 1971 Nov;108(2):782–789. doi: 10.1128/jb.108.2.782-789.1971

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

R J Griebel a,2, J M Merrick b
PMCID: PMC247141  PMID: 5001870

Abstract

Mild alkaline extraction of native poly-β-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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