Electrophoretic variation in seed proteins and interrelationships of species in the genus Oryza

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

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Electrophoretic Differences in Seed Proteins among Varieties of Soybean, Glycine max (L.) Merrill 1

Crop Science ◽

10.2135/cropsci1967.0011183x000700040008x ◽

1967 ◽

Vol 7 (4) ◽

pp. 311-313 ◽

Cited By ~ 24

Author(s):

Arnold L. Larsen

Keyword(s):

Glycine Max ◽

Seed Proteins ◽

Glycine Max L

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Identification of Hybrids from Alfalfa Crosses by Electrophoresis of Single Seed Proteins 1

Crop Science ◽

10.2135/cropsci1972.0011183x001200040047x ◽

1972 ◽

Vol 12 (4) ◽

pp. 535-537 ◽

Cited By ~ 8

Author(s):

M. K. Miller ◽

M. H. Schonhorst ◽

R. G. McDaniel

Keyword(s):

Seed Proteins ◽

Single Seed

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Impacts of Germination on the Digestibility and Quality of Pigeon pea (Cajanus cajan) Seed Proteins

10.21748/am20.97 ◽

2020 ◽

Author(s):

Ikeena Ohanenyw ◽

XIaohong Sun ◽

Chibuike Udenigwe

Keyword(s):

Cajanus Cajan ◽

Seed Proteins ◽

Pigeon Pea

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Atypical composition of seed proteins in cultivars ofPhaseolus vulgaris L.

Biologia Plantarum ◽

10.1007/bf02922804 ◽

1976 ◽

Vol 18 (3) ◽

pp. 200-205 ◽

Cited By ~ 9

Author(s):

Eva Klozová ◽

J. Kloz ◽

P. J. Winfield

Keyword(s):

Seed Proteins

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Balancing Selection on Electrophoretic Variation of Phosphoglucose Isomerase in Two Species of Field Cricket: Gryllus veletis and G. pennsylvanicus

Genetics ◽

10.1093/genetics/147.2.609 ◽

1997 ◽

Vol 147 (2) ◽

pp. 609-621

Author(s):

Laura A Katz ◽

Richard G Harrison

Keyword(s):

Balancing Selection ◽

Emergent Property ◽

Phosphoglucose Isomerase ◽

Field Cricket ◽

Nucleotide Variation ◽

Eastern United States ◽

Electrophoretic Variation ◽

Sympatric Populations ◽

Field Crickets ◽

Gryllus Veletis

Two species of crickets, Gryllus veletis and G. pennsylvanicus, share six electrophoretic mobility classes for the enzyme phosphoglucose isomerase (PGI), despite evidence from other genetic markers that the two species are not closely related within eastern North American field crickets. Moreover, the frequencies of the two most common PGI electrophoretic classes (PGI-100 and PGI-65) covary in sympatric populations of these species in the eastern United States, suggesting that PGI may be subject to trans-specific balancing selection. To determine the molecular basis of the electrophoretic variation, we characterized the DNA sequence of the Pgi gene from 29 crickets (15 G. veletis and 14 G. pennsylvanicus). Amino acid substitutions that distinguish the electrophoretic classes are not the same in the two species, and there is no evidence that specific replacement substitutions represent trans-specific polymorphism. In particular, the amino acids that diagnose the PGI-65 allele relative to the PGI-100 allele differ both between G. veletis and G. pennsylvanicus and within G. pennsylvanicus. The heterogeneity among electrophoretic classes that covary in sympatric populations coupled with analysis of patterns of nucleotide variation suggest that Pgi is not evolving neutrally. Instead, the data are consistent with balancing selection operating on an emergent property of the PGI protein.

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INTRACISTRONIC MAPPING OF ELECTROPHORETIC SITES IN DROSOPHILA MELANOGASTER: FIDELITY OF INFORMATION TRANSFER BY GENE CONVERSION

Genetics ◽

10.1093/genetics/76.2.289 ◽

1974 ◽

Vol 76 (2) ◽

pp. 289-299

Author(s):

Margaret McCarron ◽

William Gelbart ◽

Arthur Chovnick

Keyword(s):

Drosophila Melanogaster ◽

Information Transfer ◽

Large Scale ◽

Genetic Basis ◽

Xanthine Dehydrogenase ◽

Specific Protein ◽

Wild Type ◽

Electrophoretic Variation ◽

The Stability ◽

Recombination Experiments

ABSTRACT A convenient method is described for the intracistronic mapping of genetic sites responsible for electrophoretic variation of a specific protein in Drosophila melanogaster. A number of wild-type isoalleles of the rosy locus have been isolated which are associated with the production of electrophoretically distinguishable xanthine dehydrogenases. Large-scale recombination experiments were carried out involving null enzyme mutants induced on electrophoretically distinct wild-type isoalleles, the genetic basis for which is followed as a nonselective marker in the cross. Additionally, a large-scale recombination experiment was carried out involving null enzyme rosy mutants induced on the same wild-type isoallele. Examination of the electrophoretic character of crossover and convertant products recovered from the latter experiment revealed that all exhibited the same parental electrophoretic character. In addition to documenting the stability of the xanthine dehydrogenase electrophoretic character, this observation argues against a special mutagenesis hypothesis to explain conversions resulting from allele recombination studies.

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