scholarly journals The major albumin proteins from pea (Pisum sativum L). Purification and some properties

1984 ◽  
Vol 218 (3) ◽  
pp. 795-803 ◽  
Author(s):  
R R D Croy ◽  
M S Hoque ◽  
J A Gatehouse ◽  
D Boulter
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Peptide Mapping ◽  
Cytosol Fraction ◽  
Preliminary Screening ◽  
Pisum Sativum L ◽  
Terminal Amino ◽  
Cnbr Cleavage ◽  
Sulphur Amino Acids ◽  
Cotyledon Cells

A scheme is described for the fractionation of pea (Pisum sativum) albumin proteins. By using this scheme, two closely related major albumin proteins have been isolated and purified to homogeneity. The larger protein, designated PMA-L, has Mr approximately 53 000 and consists of two 25 000-Mr subunits, whereas the smaller, PMA-S, has Mr approximately 48 000 and contains two 24 000-Mr subunits. There was no evidence of mixed dimers of the two subunit sizes, despite their close homology as judged by immunological crossreaction, amino acid composition, N-terminal amino acids, tryptic-peptide mapping and CNBr-cleavage products. Both proteins contained significant amounts of sulphur amino acids. The proteins were shown to be located in the soluble cytosol fraction of cotyledon cells and are not significantly degraded on seed germination. Preliminary screening indicates the presence of homologous major albumin proteins in at least three different, though closely related, legume species.

scholarly journals Effect of water availability on changes in root amino acids and associated rhizosphere on root exudation of amino acids in Pisum sativum L.

2019 ◽  
Vol 161 ◽  
pp. 75-85 ◽  
Author(s):  
Hélène Bobille ◽  
Joëlle Fustec ◽  
Richard J. Robins ◽  
Caroline Cukier ◽  
Anis M. Limami
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Water Availability ◽  
Root Exudation ◽  
Effect Of Water ◽  
Pisum Sativum L

Release of Amino Acids from Cotyledons of Developing Seeds of Pea (Pisum sativum L.)

1989 ◽  
Vol 134 (5) ◽  
pp. 592-597 ◽  
Author(s):  
F.C. Lanfermeijer ◽  
J.W. Koerselman-Kooij ◽  
C. Kollöffel ◽  
A.C. Borstlap
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Developing Seeds ◽  
Pisum Sativum L

THE ROLE OF GLYCOSYLATED AMINO ACIDS OF WALL-BOUND PROTEIN IN CELL EXTENSION OF STEMS OF PISUM SATIVUM L. PLANTS

1978 ◽  
Vol 27 (5-6) ◽  
pp. 405-415 ◽  
Author(s):  
H. Winter ◽  
I. C. M. Wiersema ◽  
D. T. Walbrecht ◽  
H. Buffinga
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Cell Extension ◽  
Pisum Sativum L

Nutritional value of peas (Pisum sativum L.) for broilers: apparent metabolisable energy, apparent ileal amino acid digestibility and production performance

2011 ◽  
Vol 51 (2) ◽  
pp. 150 ◽  
Author(s):  
C. L. Nalle ◽  
V. Ravindran ◽  
G. Ravindran
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Pisum Sativum ◽  
Digestive Tract ◽  
Soybean Meal ◽  
Nutritional Value ◽  
Production Performance ◽  
Partial Replacement ◽  
Pisum Sativum L ◽  
Metabolisable Energy

Two experiments were conducted to evaluate the nutritional value of four cultivars (Santana, Miami, Courier and Rex) of peas (Pisum sativum L.) for broilers. In Experiment 1, the apparent metabolisable energy (AME) and the apparent ileal amino acid digestibility of these four cultivars were determined. The cultivar effects were found to be not significant (P > 0.05) for the AME and apparent ileal digestibility of amino acids, with the exception of arginine, which was lower (P < 0.05) in Courier than other cultivars. In Experiment 2, using the energy and digestible amino acid values determined in Experiment 1, diets containing 200 g/kg of the four cultivars of peas were formulated and the effects of feeding these diets on the performance and digestive tract development of broiler starters was investigated. Weight gain, feed intake and feed per gain of broiler starters fed diets containing peas were similar (P > 0.05) to those fed the maize-soybean meal diet. In general, the digestive tract development was unaffected (P > 0.05) by the inclusion of peas. The excreta scores of birds fed diets based on Santana, Miami and Rex were similar (P > 0.05) and that of the Courier-based diet was lower (P < 0.05) than those fed the maize-soy control diet. These results suggest that peas are good sources of metabolisable energy and digestible amino acids, and that they can be included at 200 g/kg level as a partial replacement for soybean meal in broiler starter diets without adverse effects on performance.

Elicitation of Pisatin in Pea (Pisum sativum L.) By Copper-Asparagine Complexes

1987 ◽  
Vol 14 (5) ◽  
pp. 549 ◽  
Author(s):  
IAM Cruickshank ◽  
WF Dudman ◽  
MB Peoples ◽  
MM Smith
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Aspartic Acid ◽  
Topical Application ◽  
Mode Of Action ◽  
Amino Nitrogen ◽  
Plant Cells ◽  
The Other ◽  
Pisum Sativum L ◽  
H 20

The early events in the mode-of-action of CuCl2 solutions in relation to pisatin elicitation were examined. Cu2+ ions were rapidly adsorbed to or taken up by pea endocarp tissue from CuCl2 solutions and large quantities of amino acids and sugars were rapidly released from the plant cells into the external solutions. Asparagine accounted for 56% of the amino-nitrogen while glucose represented 58% of the sugars. The concentration increases of asparagine and glucose relative to the water controls were approximately 140- and 180-fold respectively. The enhanced pisatin elicitor activity of pea-Cu2+ -leachates (4 h, 20°C) obtained following the topical application of CuCl2 solutions to endocarp tissues was primarily due to the formation in the external solutions of Cu2+ -asparagine complexes. This was demonstrated by their isolation, identification and bioassay, and by the bioassay of synthetic Cu2+ -asparagine complexes. Cu2+ - complexes with other amino acids also present in pod leachates were prepared and their differential pisatin elicitor activity compared to asparagine. Only aspartic acid-complexes exhibited higher elicitor activity (109%) than Cu2+-asparagine. The other amino acids used resulted in pisatin concentrations 64 (homoserine) to 78% (glutamine) of that induced by asparagine.

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