Amino acid composition of seed proteins of Lupinus albus

1979 ◽  
Vol 27 (5) ◽  
pp. 977-978 ◽  
Author(s):  
Marcello Duranti ◽  
Paolo Cerletti
1975 ◽  
Vol 26 (8) ◽  
pp. 1237-1246 ◽  
Author(s):  
Tumkur K. Virupaksha ◽  
Geeta Ramachandra ◽  
Dasasetty Nagaraju

1969 ◽  
Vol 47 (12) ◽  
pp. 1857-1863 ◽  
Author(s):  
Oluf L. Gamborg ◽  
A. J. Finlayson

Amino acid analyses were performed on the soluble and total proteins from plant cells grown in suspension culture. The cell cultures originated from 12 different plant species, and the explants were taken from different organs of the plants.Relatively small differences in the amino acid composition existed between the soluble proteins from different species, between cells originating from different organs of the same species, and between the same cultures grown on different media under the same environmental conditions.There was some variation in the proportion of basic, aromatic, and sulfur-containing amino acids which constituted about 17%, 9.5%, and 3% of the protein amino acids, respectively. The amino acid composition of the soluble proteins of wheat coleoptile and soybean hypocotyl resembled that of the soluble proteins from cultured cells of these plants. Essential amino acids, particularly the basic ones and methionine, were proportionally higher in the cell proteins than those reported for seed proteins.


1988 ◽  
Vol 51 (1) ◽  
pp. 5-12 ◽  
Author(s):  
Peter R. Shewry ◽  
Saroj Parmar ◽  
Julian Franklin ◽  
Rodger White

SummaryThe hordein polypeptide controlled by the Hrd G (Hor 4) locus in Elgina and derived lines was purified by preparative isoelectric focusing. The amino acid composition was similar to those of the major B hordeins encoded by the Hor 2 locus. Genetic analysis confirmed that Hor 4 is located proximally to Hor 1 on the short arm of chromosome 5. It is speculated that Hor 4 arose by translocation of genes from Hor 2, possibly in an ancestor of Elgina.


1992 ◽  
Vol 40 (6) ◽  
pp. 931-936 ◽  
Author(s):  
Ana P. Barba de la Rosa ◽  
Jacques. Gueguen ◽  
Octavio. Paredes-Lopez ◽  
Gerard. Viroben

1987 ◽  
Vol 7 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Yogesh R. Mawal ◽  
Madhumalti R. Mawal ◽  
P. K. Ranjekar

Rice albumin from Oryza sativa (Var. Basmati 370) accounts for about 5% of the total seed proteins. A major fraction of rice albumin has been found to be a glycoprotein which is a monomer of 60 kd having iso-electric point 6.54. When rice albumin is digested with trypsin, it shows the presence of 24 peptides as against 28 peptides which were estimated from its amino acid Composition. This indicates the presence of a few peptides which resemble each other in their charge and Rf values. Antibodies against Con A purified rice albumin were affinity purified and were used to quantitate the rice albumin levels during post-anthesis by RIA and ELISA. The latter experiments reveal that maximum albumin is present between 18 and 20 days post-anthesis.


2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton

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