Glutamate Synthetase in Developing Cotyledons of Pisum sativum

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Synthesis and Interconversion of Amino Acids in Developing Cotyledons of Pea (Pisum sativum L.).

Freshly isolated cotyledons from 10-day developing pea (Pisum sativum) seeds were fed radiolabeled precursors for 5 hours, and the specific radioactivity of the free and total protein amino acids was determined using a dansylation procedure. When the seven most abundant amino acids in phloem exudate of pea fruits (asparagine, serine, glutamine, homoserine, alanine, aspartate, glycine) were fed ...

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The Influence of Axis Removal on Protein Metabolism in Cotyledons of Pisum sativum L.

The protein metabolism of cotyledons attached to the embryonic axis has been compared with that in cotyledons removed from the axis at the initiation of a 6-day imbibition. Total protein declined in the attached but not in the detached cotyledons. Concurrent with the decline in protein level in the intact cotyledons there was an increased capacity to incorporate exogenously supplied leucine int...

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Glycoprotein Metabolism in the Cotyledons of Pisum sativum during Development and Germination.

The glycoprotein nature of legumin and vicilin, the reserve globulins in the cotyledons of Pisum sativum was studied. Legumin from mature seed was found to contain 1% neutral sugars (mannose and glucose) and 0.1% amino sugar (glucosamine), whereas vicilin contained 0.3% neutral sugar (mannose) and 0.2% amino sugar (glucosamine). On the basis of the incorporation of (14)C-labeled glucosamine, it...

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Asparaginase Isolated from Developing Seeds of Pisum sativum

Asparaginase (EC 3.5.1.1) was isolated from the developing seed of Pisum sativum. The enzyme is dependent upon the presence of K+ for activity, although Na+ and Rb+ may substitute to a lesser extent. Maximum activity was obtained at K+ concentrations above 20 millimolar. Potassium ions protected the enzyme against heat denaturation. The enzyme has a molecular weight of 68,300. Asparaginase acti...

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The 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...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1976

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.57.6.862