Processing Pisum sativum seed storage protein precursors in vitro
نویسندگان
چکیده
منابع مشابه
Control of storage-protein synthesis during seed development in pea (Pisum sativum L.).
The tissue-specific syntheses of seed storage proteins in the cotyledons of developing pea (Pisum sativum L.) seeds have been demonstrated by estimates of their qualitative and quantitative accumulation by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and rocket immunoelectrophoresis respectively. Vicilin-fraction proteins initially accumulated faster than legumin, but whereas legu...
متن کاملCharacterization of pea (Pisum sativum) seed protein fractions.
BACKGROUND Legume seed proteins have to be chemically characterized in order to properly link their nutritional effects with their chemical structure. RESULTS Vicilin and albumin fractions devoid of cross-contamination, as assessed by mass peptide fingerprinting analysis, were obtained from defatted pea (Pisum sativum cv. Bilbo) meal. The extracted protein fractions contained 56.7-67.7 g non-...
متن کاملPolyadenylate-Binding Protein from Pea (Pisum sativum)'
A polyadenylate-binding protein (PABP) was purified from cellfree extracts prepared from pea seedlings (Pisum sativum) by ammonium sulfate precipitation and Affi-Gel Blue and polyadenylate-Sepharose 4B affinity chromatography. The final preparation from polyadenylate-Sepharose 4B columns contained a single 70-kilodalton polypeptide with high polyadenylate-binding activity. The purified protein ...
متن کاملMeasurement of gene number for seed storage proteins in Pisum.
We have measured the numbers of genes coding for the three seed storage proteins, vicilin, convicilin and legumin, in a number of Pisum genotypes of variant protein composition. No difference in gene number existed among P. sativum genotypes for any of the proteins. There were differences in the number of genes coding for individual proteins with approximately 11 genes (per haploid genome) for ...
متن کاملDNA methylase from Pisum sativum.
DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleoti...
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ژورنال
عنوان ژورنال: Cell Research
سال: 1990
ISSN: 1001-0602,1748-7838
DOI: 10.1038/cr.1990.15