scholarly journals Cell-free Synthesis of Pea Seed Proteins

1977 ◽  
Vol 60 (5) ◽  
pp. 655-661 ◽  
Author(s):  
Thomas J. V. Higgins ◽  
Donald Spencer
Keyword(s):  
PROTEOMICS ◽  
2011 ◽  
Vol 11 (19) ◽  
pp. 3942-3942 ◽  
Author(s):  
Michael Bourgeois ◽  
Françoise Jacquin ◽  
Florence Cassecuelle ◽  
Vincent Savois ◽  
Maya Belghazi ◽  
...  

PROTEOMICS ◽  
2011 ◽  
Vol 11 (9) ◽  
pp. 1581-1594 ◽  
Author(s):  
Michael Bourgeois ◽  
Françoise Jacquin ◽  
Florence Cassecuelle ◽  
Vincent Savois ◽  
Maya Belghazi ◽  
...  

2021 ◽  
Author(s):  
Sandeep Kaur Dhaliwal ◽  
Pooja Salaria ◽  
Prashant Kaushik

Grain legumes are well known as staple sources of soluble protein worldwide. Pea is essentially the most quickly growing crop for immediate human consumption and has the potential for higher effect as being a protein supply for foods processing apps. Pea seeds are an essential source of plant-based proteins. The better acceptance of pea protein-rich food is due to pea manifold attributes, excellent functional qualities, high vitamin value, accessibility, and comparatively small cost. Pea proteins are not merely nutritional amino acids but are an indispensable source of bioactive peptides that offer health benefits. This chapter focuses on the present information of isolation methods, extraction, and of seed proteins in pea. Overall, we believe that analogous research and advancement on pea proteins would be required for further more substantial increase in pea protein utilization is envisaged.


1998 ◽  
Vol 8 (3) ◽  
pp. 367-375 ◽  
Author(s):  
Eduardo Marentes ◽  
Michael A. Grusak

AbstractTo understand the cellular processes related to iron transport and sequestration within the developing pea seed (Pisum sativum), total iron and ferritin iron were analysed in seed coat and embryo tissues of the iron-hyperaccumulating pea mutant, Sparkle [dgl, dgl], and its wild-type parent, cv. Sparkle. For plants grown hydroponically with 2 μM Fe, embryo Fe concentrations averaged 65 μg g−1 dry weight in mature wild-type seeds and 163 μg g−1 dry weight in mature dgl seeds; iron concentrations were also higher in dgl seed coats. Extracted and electrophoretically separated seed proteins were probed with a polyclonal antibody raised against pea seed ferritin. In both genotypes, ferritin was detected in the embryo, but not in the seed coat. Ferritin iron accounted for 92% of the total iron in mature wild-type embryos, but only 42% of the total iron in mature dgl embryos. Radiotracer studies using 59Fe were used to characterize the movement of iron within the seed coat. Unequal distribution of 59Fe in opposing sections taken from the two hemispheres of the seed coat demonstrated that iron was symplastically phloem unloaded. These results suggest that iron resides transiently within the nonvascular seed coat cells and that all cells at the inner surface of the seed coat may be involved in the release of iron to the embryo apoplast. However, the form of iron resident within the seed coat and/or taken up by the embryo is presently unknown.


1984 ◽  
Vol 75 (3) ◽  
pp. 651-657 ◽  
Author(s):  
Peter M. Chandler ◽  
Donald Spencer ◽  
Peter J. Randall ◽  
Thomas J. V. Higgins

2018 ◽  
Vol 30 (2) ◽  
pp. 19-28
Author(s):  
A. J. Oludare ◽  
J. I. Kioko ◽  
A. A. Akeem ◽  
A. T. Olumide ◽  
K. R. Justina ◽  
...  

Nine accessions of Bambara groundnut (Vigna subterranea (L.) Verdc.,syn. Voandzeia subterranea (L.) Thouars ex DC.)  obtained from National Centre for Genetic Resources and Biotechnology (NACGRAB), Ibadan, Oyo state, were assessed for their genetic and phylogenetic relatedness through electrophoretic analysis of the seed proteins. 0.2g of the seeds were weighed and macerated with mortar and pestle in 0.2M phosphate buffer containing 0.133M of acid (NaH2PO4) and 0.067 of base (Na2HPO4) at pH 6.5. Protein characterization with standard marker revealed that the seeds of the nine accessions contained proteins (B.S.A, Oval Albumin, Pepsinogen, Trypsinogen and Lysozyme) with molecular weights ranging from 66kda and above, 45 – 65 kDa, 44 – 33 kda, 32-24 kDa and 23-14 kDa, respectively. The student T-test revealed that accessions B, C, E, F, H and I have molecular weights not significantly different from one another (P<0.05) while samples A, D and G showed significantly different values (P>0.05). All the accessions had at least two proteins and two major bands in common. The study revealed intra-specific similarities and genetic diversity in protein contents among the nine accessions of Bambara groundnut (Vigna subterraranea (L.) Verdc.syn


Crop Science ◽  
1972 ◽  
Vol 12 (4) ◽  
pp. 535-537 ◽  
Author(s):  
M. K. Miller ◽  
M. H. Schonhorst ◽  
R. G. McDaniel
Keyword(s):  

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