l-Canavanine Transport and Utilization in Developing Jack Bean, Canavalia ensiformis (L.) DC. [Leguminosae].

نویسندگان

  • G A Rosenthal
  • D Rhodes
چکیده

l-Canavanine, the guanidinooxy structural analog of l-arginine, is an important nonprotein amino acid of many leguminous plants with nitrogen storage a major proported role. l-[Guanidinooxy-(14)C]canavanine, [(14)C] urea, and [(15)N]urea were injected separately into the fleshy, green cotyledons of 9-day old jack bean plants, Canavalia ensiformis (L.) DC. [Leguminosae]. There was significant transport of canavanine from the cotyledons to the aboveground portions of the plant, but not to the roots. Within 1.5 hours of isotope administration, the remaining labeled canavanine was divided equally between the cotyledons and the aboveground portions of the plant. During the 48-hour postinjection period, the contribution of l-[guanidinooxy-(14)C]canavanine to the total (14)carbon of the cotyledons decreased rapidly while it increased in the aboveground portions of the plant.[(14)C]Urea is degraded very rapidly; only 4.4% of the initial dose remained after 1.5 hours. Urea is catabolized so effectively within the cotyledons that not even 2% of the administered urea can be detected in tissues outside of these storage organs. [(15)N]Urea supplied to the developing coytledons leads to rapid (15)N incorporation into the amino nitrogen of glutamic acid and/or glutamine (28% (15)N abundance after 3 hours). Other amino acids are labeled but less heavily. The data are consistent with the proported role for l-canavanine of nitrogen storage within the developing cotyledons and cotyledonary canavanine is transported very effectively to the aboveground portions of the plant. It is not yet clear how efficiently this transported canavanine supports the nitrogen metabolism of the developing plant.

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منابع مشابه

Investigations of Canavanine Biochemistry in the Jack Bean Plant, Canavalia ensiformia (L.) DC: I. Canavanine Utilization in the Developing Plant.

An ontogenetic study of the canavanine and soluble protein pools in the developing jack bean plant, Canavalia ensiformis (L.) DC., was conducted. Evidence was presented which clearly established the conversion of canavanine to canaline and urea as the principal pathway of canavanine utilization. The catabolic reactions of certain bacteria involving the formation of guanidine or hydroxyguanidine...

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l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. (Leguminosae).

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Investigations of Canavanine Biochemistry in the Jack Bean Plant, Canavalia ensiformis (L.) DC: II. Canavanine Biosynthesis in the Developing Plant.

The canavanine content of developing leaves of jack bean, Canavalia ensiformis (L.) DC., increases during leaf development. The leaf possesses the enzymes required for synthesizing canavanine by a cyclic series of reactions analogous to the ornithine-urea cycle. This reaction series involves the sequential formation of canaline, O-ureidohomoserine, and canavaninosuccinic acid.

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An Ontogenetic Study of Canavanine Formation in the Fruit of Jack Bean, Canavalia ensiformis (L.) DC.

An ontogenetic study of canavanine formation in the fruit of jack bean, Canavalia ensiformis (L.) DC. was conducted. Evidence was presented to show that the ovary wall is the reservoir for seed canavanine. The testa possesses sufficient canavanine to account for the continued elevation in seed canavanine after the pod senesces. The seed canavanine concentration is not constant inasmuch as the c...

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l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr.

Studies have been conducted with the arginase (l-arginine amidinohydrolase, EC 3.5.3.1) of two legumes: jack bean, Canavalia ensiformis (L.) DC., a l-canavanine-containing plant and soybean, Glycine max, a canavanine-free species. Analyses of the arginase obtained from gradient-purified mitochondria of these legumes revealed that the arginine-dependent (ADA) and canavanine-dependent activities ...

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عنوان ژورنال:
  • Plant physiology

دوره 76 2  شماره 

صفحات  -

تاریخ انتشار 1984