Precursors of storage proteins in Lupinus angustifolius

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Precursors of storage proteins in Lupinus angustifolius.

The proteins that are synthesized during differentiation and development in the cotyledons of Lupinus angustifolius L. were characterized both in situ and after purification. The proteins present in situ were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and subjected to 'Western'-blot analysis to identify immunologically related polypeptides. The major storage protein...

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The aspartate aminotransferase-P2 gene from Lupinus angustifolius.

and plays a key role in carbon and nitrogen metabolism in plants. The enzyme has been shown to be involved in the shuttling of reducing equivalents from the cytoplasm to chloroplasts, mitochondria, glyoxysomes, and peroxisomes via the malate-aspartate shuttle (Wightman and Forest, 1978). Up to five separate isoforms of AAT have been reported in plants, differing both kinetically and in levels a...

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Alkaloid Content Variations in Lupinus Luteus L. and Lupinus Angustifolius L

Testing of lupine varieties for alkaloids was performed in the period 2006-2010 at the Voke Branch of the Lithuanian Institute of Agriculture in the course of a competitive trial of feeding lupine (Lupinus sp.). Samples of feeding yellow lupine (Lupinus luteus L.) varieties as well as narrow-leaved lupine (Lupinus angustifolius L.) were used. The alkaloid concentration was assessed in the perio...

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The energy value of Lupinus angustifolius and Lupinus albus for growing pigs

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Characterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifolius.

Site-directed mutagenesis has been used to characterize the functions of key amino acid residues in the catalytic site of the 'nudix' hydrolase, (asymmetrical) diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) hydrolase (EC 3.6.1.17) from Lupinus angustifolius, the three-dimensional solution structure of which has recently been solved. Residues within the nudix motif, Gly-(Xaa)5-Glu-(Xaa)7-Arg-Glu...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1984

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2210333