Amino Acid Release from the Seed Coat of Developing Seeds of Vicia faba and Pisum sativum
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چکیده
منابع مشابه
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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Differential and sucrose density gradient centrifugation established that about 80% of the total arginase activity (EC 3.5.3.1) in cotyledons of germinating broad bean seeds (Vicia faba L.) was present in the mitochondrial fraction. The mitochondrial arginase activity was enhanced considerably by exposure to osmotic shock, by freezing and thawing, or by Triton X-100 treatment. About 10% of the ...
متن کاملAmino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin.
The iron storage protein, ferritin, is widely distributed in the living kingdom. Here the complete cDNA and derived amino-acid sequence of pea seed ferritin are described, together with its predicted secondary structure, namely a four-helix-bundle fold similar to those of mammalian ferritins, with a fifth short helix at the C-terminus. An N-terminal extension of 71 residues contains a transit p...
متن کاملGene Function Expression Profile of Faba bean (Vicia faba) Seeds
Faba bean (Vicia faba L) is one of the important grain crops worldwide and its genome, the largest among grain legumes (approx. 13.4 Gb), has yet to be sequenced. Comprehensive knowledge of genes expressed in the crop's large seeds would not only help drive new genetic improvements in the crop but also aid its future genome characterization. Here, we applied high throughput RNASeq (Quantificati...
متن کاملSubtilisin Inhibitor from Seeds of Broad Bean (vicia Faba); Purification, Amino Acid Sequence and Specificity of Inhibition
A potent inhibitor of microbial serine proteases, including subtilisin, has been purified 1100-fold from seeds of broad bean (Vicia faba, cv. Kleine Thtiringer). Chymotrypsin and trypsin were not inhibited, but a weak "temporary" inhibition of pancreas elastase was observed. The preparation of pure inhibitor contained one major molecular form with a blocked N-terminal (MW 10,000, pl 4.8) and a ...
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ژورنال
عنوان ژورنال: Annals of Botany
سال: 1985
ISSN: 1095-8290,0305-7364
DOI: 10.1093/oxfordjournals.aob.a086903