Yariability of dry seed mycobiota of Pisum sativum
نویسندگان
چکیده
منابع مشابه
Characterization 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 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 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...
متن کاملThe cDNA cloning of a pea (Pisum sativum) seed lipoxygenase. Sequence comparisons of the two major pea seed lipoxygenase isoforms.
Cloning and sequencing of two cDNAs from mRNA of maturing pea (Pisum sativum) seeds allowed the deduction of the complete amino acid sequence of a lipoxygenase polypeptide which is most similar to that of soya-bean lipoxygenase 2. The predicted Mr of this polypeptide is 97134, and its sequence permits comparisons between the lox2-type and the lox3-type lipoxygenase isoforms from pea and soya be...
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...
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ژورنال
عنوان ژورنال: Acta Mycologica
سال: 2014
ISSN: 2353-074X
DOI: 10.5586/am.1998.008