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

Abstract:

: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). 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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Griebel RJ,Merrick JM

doi

10.1128/JB.108.2.782-789.1971

subject

Has Abstract

pub_date

1971-11-01 00:00:00

pages

782-9

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

108

pub_type

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