Genetically Controlled Electrophoretic Variants of a Storage Protein in Pisum Sativum
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چکیده
منابع مشابه
Polyadenylate-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 کاملControl 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 کاملThe isoperoxidases of Pisum sativum.
The heterogeneity of the peroxidases in peas was examined by starch gel electrophoresis. Comparisons were made between tall and dwarf cultivars and among organ systems developed in light and darkness. Isoperoxidase bands could be grouped as cathodic, anodic and near-neutral (at pH 9.0) types. The cathodic set stained well with guaiacol oxidation products whereas some anodic bands reacted prefer...
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 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: Australian Journal of Biological Sciences
سال: 1968
ISSN: 0004-9417
DOI: 10.1071/bi9680827