Asparagine Formation in Soybean Nodules
نویسندگان
چکیده
منابع مشابه
Asparagine formation in soybean nodules.
(15)NH(4) (+) and [(15)N](amide)-glutamine externally supplied to detached nodules from soybean plants (cv. Tamanishiki) were incorporated within nodule tissues by vacuum infiltration and metabolized to various nitrogen compounds during 60 minutes of incubation time. In the case of (15)NH(4) (+) - feeding, the (15)N abundance ratio was highest in the amide nitrogen of glutamine, followed by glu...
متن کاملAsparagine biosynthesis in soybean nodules.
Asparagine biosynthesis in soybean (Glycine max [L.] Merr.) nodules has been difficult to demonstrate due to the poor conversion of suspected immediate precursors to asparagine and the instability of the key enzyme asparagine synthetase. The present study was designed to explore the effects of two ammonium assimilation inhibitors on the metabolism of (14)CO(2) to [(14)C]asparagine and to demons...
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Asparaginase activity (</=1 mumol/mg protein . hr) was detected in extracts of soybean (Glycine max [L.] Merr.) leaf blades, but, even after efforts to optimize extraction and assay of the enzyme, specific activity was not sufficient to metabolize the estimated amount of asparagine translocated to leaves. Asparagine transaminase activity with glyoxylate or pyruvate was at least 52 and 62 nmol/m...
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SUCROSE SYNTHASE (UDPGLUCOSE: d-fructose 2-alpha-d-glucosyl transferase, EC 2.4.1.13) has been purified from the plant cytosolic fraction of soybean (Glycine max L. Merr cv Williams) nodules. The native enzyme had a molecular weight of 400,000. The subunit molecular weight was 90,000 and a tetrameric structure is proposed for soybean nodule sucrose synthase. Optimum activity in the sucrose clea...
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Nodule extracts prepared from Glycine max var Woodworth possessed endopeptidase, aminoptidase, and carboxypeptidase actiities. Three distinct endopeptidase activities could be resolved by disc-gel electrophoresis at pH 8.8. According to their order of increasing electrophoretic mobility, the first of these enzymes hydrolyzed azocasein and n-benzoyl-LLeu-p8-naphthylamide, while the second hydrol...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1980
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.66.1.139