| Literature DB >> 16663605 |
Abstract
The association of endoproteolytic activity with purified ribulose bisphosphate carboxylase (RuBPCase) from barley (Hordeum vulgare var Numar) leaves was investigated. RuBPCase purified by chromatography on agarose gel and diethylaminoethyl-cellulose was free of associated endoproteolytic activity. The addition of leupeptin and casein to the extraction buffer completely eliminated proteolysis during initial extraction of RuBPCase. Endoproteolytic activity previously found associated with RuBPCase was identified as being due to contamination of endoproteinases from broken vacuoles.Entities:
Year: 1984 PMID: 16663605 PMCID: PMC1066837 DOI: 10.1104/pp.75.1.74
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340