New knowledge about the PHA-locus and P(3HB) granule-associated proteins in Chromatium vinosum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-06

AUTHORS

Matthias Liebergesell, Alexander Steinbüchel

ABSTRACT

The isolation of poly(3-hydroxybutyric acid) granules of Chromatium vinosum D was re-examined. Beside the PHA synthase and a 17 kDa protein, a 14 kDa protein was identified as predominant granule-associated protein. The Mr as well as the N-terminal amino acid sequence exhibited identity to ORF5Cv, which is located within the pha-locus of C. vinosum. In addition, sequence alignements revealed new information about ORF4Cv, which is also located within the pha-locus, and about the 17 kDa protein, which exhibited homology to heat shock proteins recently detected in Escherichia coli. More... »

PAGES

719-724

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00130772

DOI

http://dx.doi.org/10.1007/bf00130772

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1018079936


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