SDS–PAGE of seed proteins in Festuca (Poaceae): taxonomic implications

1991 ◽  
Vol 69 (7) ◽  
pp. 1425-1432 ◽  
Author(s):  
S. G. Aiken ◽  
S. E. Gardiner
Keyword(s):  
Native Species ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Banding Patterns ◽  
Ungerminated Seed ◽  
Sds Page ◽  
Species Specific

Taxonomically useful descriptors were provided by the banding patterns of seed storage proteins obtained when extracts of bulked, ungerminated seed samples from commercially available North American native species of Festuca were analyzed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS–PAGE). The banding patterns for three species of rough fescues (section Breviaristatae Krivot) indicate that although the taxa are closely related, F. campestris Rydb. (2n = 56) does not appear to be an autoploid of either F. altaica Trin. (2n = 28) or F. hallii (Vasey) Piper (2n = 28). A distinct band corresponding to a molecular weight of 57 000 occurred in the seed protein profiles of all native and commercial samples of Festuca L. analyzed. The profile for F. californica Vasey, questionably section Breviaristatae, also has a band at this position, and is very different from that of F. altaica, F. campestris, and F. hallii. Species-specific banding patterns were observed for F. brachyphylla Schultes, F. saximontana Rydb., F. idahoensis Elmer, and F. trachyphylla (Hackel) Krajina (F. ovina L. s.l., F. longifolia Thuill., F. ovina var. duriuscula auct. amer.). The results support the recognition of subgenus Schedonorus (Beauv.) Peter., and sections Breviaristatae Krivot and Festuca. Key words: Poaceae, Festuca, SDS–PAGE seed proteins.

Revealing genetic diversity in land races and wild accessions of mungbean [Vigna radiata (L.) Wilczek] using SDS-PAGE of seed storage proteins

2015 ◽  
Author(s):  
Ananya Panda ◽  
Swapan K. Tripathy
Keyword(s):  
Storage Proteins ◽  
Seed Storage Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Land Races ◽  
Sds Page ◽  
Wild Accessions ◽  
Total Seed

Total seed storage protein profiles of 74 mungbean land races, three wild accessions and a popular variety ‘Jyoti’ of Odisha were analysed by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). 32 genotypes could be clearly identified based on genotype-specific seed protein fingerprints while rest of the test genotypes were categorized into eight protein types. Genotypes included in each protein type had 100% homology and some of these could be duplicates. In this pursuit, a few specific polypeptide markers have been detected for identification of the land races/ genotypes. Dendrogram based on electrophoretic data clustered the genotypes into seven groups at 70% phenon level. Paralakhemundi local, Samarjhola local and Phulbani local-D; and three wild accessions (TCR 20, TCR 213 and TCR 243) were comparatively divergent from other genotypes. Besides, Jyoti, Kalahandi local 2A, Sikri local, kodala local A and TCR 20 were identified to be protein rich with high seed yield. TCR 20 being morphologically similar to mungbean, moderately high protein content and high yielding as well as resistant to drought and bruchids; it may serve as a valuable source genotype in recombination breeding

Identification of timothy cultivars by SDS-PAGE analysis of seed storage proteins

1992 ◽  
Vol 72 (4) ◽  
pp. 1215-1222 ◽  
Author(s):  
Q. Cai ◽  
M. R. Bullen
Keyword(s):  
Storage Proteins ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Phleum Pratense ◽  
Environmental Stability ◽  
Blue Staining ◽  
Coomassie Blue Staining ◽  
Coomassie Blue ◽  
Sds Page

SDS-PAGE analysis of seed proteins was carried out to identify the cultivars in the forage crop, timothy (Phleum pratense L.). Nineteen cultivars of timothy were examined. Among them five were from Europe and fourteen from North America. In total fifty protein bands were detected in mature seed extract by SDS-PAGE followed by Coomassie blue staining. Except for two pairs, all the cultivars were differentiated by SDS-PAGE analysis of seed storage proteins. In the electrophoretic profile, no protein bands were found to be specific either to European or to North American cultivars which is an indication of their genetic similarity. Twelve samples of cultivar Toro harvested from Alberta and Manitoba (Canada), Idaho and Minnesota (USA) were compared and no significant differences were found in their seed protein banding patterns, which suggests environmental stability of timothy seed proteins.Key words: SDS PAGE, timothy cultivar identification, seed storage proteins

Placement of loci for avenins and resistance to Puccinia coronata to a common linkage group in Avena strigosa

Genome ◽  
1994 ◽  
Vol 37 (6) ◽  
pp. 900-903 ◽  
Author(s):  
P. J. Rayapati ◽  
V. A. Portyanko ◽  
M. Lee
Keyword(s):  
Linkage Group ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Puccinia Coronata ◽  
A Genome ◽  
Genes Encoding ◽  
Group 1 Chromosomes

Alcohol-soluble seed storage proteins of oat (avenins) were extracted from two diploid accessions representing the A genome and separated by high-resolution acid polyacrylamide gel electrophoresis. Polymorphisms were detected for three clearly resolved protein bands. Linkage analysis of 88 F2:3 families mapped the three bands to a single locus. Integration of avenin segregation data with an RFLP linkage map constructed from the same population, mapped the avenin locus to a linkage group containing a locus conferring resistance to nine isolates of Puccinia coronata. Linkage between genes encoding alcohol-soluble seed proteins and genes for resistance to Puccinia species was also observed for the homoeologous group 1 chromosomes of barley (1H), rye (1R), wheat (1A, 1B, 1D), and chromosomes 4 and 10 of maize.Key words: genetics, seed protein, disease resistance.

scholarly journals Seed storage proteins in coffee

2001 ◽  
Vol 13 (1) ◽  
pp. 33-40 ◽  
Author(s):  
SANDRA M. T. BAÚ ◽  
PAULO MAZZAFERA ◽  
LUIZ G. SANTORO
Keyword(s):  
Molecular Weight ◽  
Storage Proteins ◽  
Protein A ◽  
Gel Filtration ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Sds Page ◽  
Reserve Protein ◽  
Coffee Species

It has been reported that Coffea arabica seeds contain as the main reserve protein, a legumin-like protein, constituted of two subunits, alpha and beta, of approximately 35 and 20 kDa. In this work the seed proteins of several coffee species and varieties were investigated by SDS-PAGE and gel filtration. No differences were observed in the electrophoretic profiles among varieties of C. arabica, however, marked differences were observed among species, or even among individuals of some species. In general, the molecular weight of the subunits alpha and beta accounted for a monomer of 48 to 62 kDa. However, native molecular weight obtained by gel filtration showed that for most of the species there is association of 6 of such proteins, in a hexamer. The most marked difference was observed for C. canephora and C. racemosa. The former clearly showing isoforms of the subunits, and the later showing absence of the beta subunit. The influence of proteases in this observations is discussed.

scholarly journals Genetic Diversity of Common Bean Genotypes as Revealed By Seed Storage Proteins and Some Agronomic Traits

2014 ◽  
Vol 67 (1) ◽  
pp. 125-137 ◽  
Author(s):  
Akbar Marzooghian ◽  
Mohammad Moghaddam ◽  
Mostafa Valizadeh ◽  
Mohammad Hasan Kooshki
Keyword(s):  
Genetic Diversity ◽  
Common Bean ◽  
Yield Components ◽  
Storage Proteins ◽  
Agronomic Traits ◽  
Morphological Characteristics ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Seed Morphology

AbstractEvaluation of the genetic diversity present within species is essential for conservation, management and utilization of the genetic resources. The objective of this study was to evaluate genetic variability of 70 common bean genotypes for seed storage proteins, grain morphological characteristics and agronomic traits. Two methods of extracting soluble seed proteins in salt were used.Positive correlations were observed among both seed morphological characters and developmental characters while yield components showed negative correlations with each other. Factor analysis for agronomic and grain morphological traits resulted in three factors were named yield components, seed morphology and phenology, respectively. Most genotypes had lower or medium scores for yield components and phenology factors. Considerable diversity was observed for seed morphology factor among the common bean genotypes.Nei’s diversity coefficient (He= 0.4), effective number of alleles (Ae= 1.69) and number of polymorphic loci (N = 17) indicated larger variation in the extraction method of soluble proteins in low salt (0.2 M NaCl) than high salt (1 M NaCl) condition. Considering that the centers of diversity for common bean are different in seed size, the result of Gst statistics showed that bands with relative mobility of 30, 32, 38 and 40 differentiated two weight groups more than other bands. Furthermore, significant differences were observed between these bands for number of pods per plant and number of seeds per plant.

scholarly journals Isolation and properties of a metalloproteinase from buckwheat (Fagopyrum esculentum) seeds

1990 ◽  
Vol 272 (3) ◽  
pp. 677-682 ◽  
Author(s):  
M A Belozersky ◽  
Y E Dunaevsky ◽  
N E Voskoboynikova
Keyword(s):  
Storage Proteins ◽  
Limited Proteolysis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Fagopyrum Esculentum ◽  
Gel Chromatography ◽  
Ph Optimum ◽  
Peptide Bonds ◽  
Sds Page ◽  
Homogeneous Preparation

A homogeneous preparation of metalloproteinase, purified 1000-fold, was obtained from buckwheat (Fagopyrum esculentum) seeds. The Mr of the enzyme, determined by SDS/PAGE, was 34,000 (it was 39,000 by gel chromatography). Its pH optimum was 8.0-8.2 with 13 S globulin, from buckwheat seeds, as substrate. Atomic-absorption spectroscopy revealed the presence of one Zn2+ ion per enzyme molecule. The enzyme was completely inhibited by EDTA (1 mM), zincone (1 mM) and 1, 10-phenanthroline (1 mM). The metalloproteinase performed limited proteolysis of the following seed storage proteins: 13 S globulin from buckwheat seeds and 11 S globulin from soybean (Glycine max) seeds. It hydrolysed three peptide bonds formed by the amino groups of Leu15, Tyr16 and Phe25 in the oxidized B-chain of insulin. In its main properties the enzyme is similar to metalloproteinases of animal and bacterial origin.

scholarly journals Mobilization of seed storage proteins is crucial to high vigor in common bean seeds

2022 ◽  
Vol 52 (2) ◽  
Author(s):  
Natalia Carolina Moraes Ehrhardt-Brocardo ◽  
Cileide Maria Medeiros Coelho
Keyword(s):  
Storage Proteins ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Seed Vigor ◽  
Intensity Difference ◽  
Biochemical Component ◽  
Germination Process ◽  
Radicle Protrusion ◽  
Relationship Of

ABSTRACT: Seed germination is a complex process controlled by many factors, in which physical and biochemical mechanisms are involved and the mobilization of reserves is crucial for this process to occur. Although, seed reserve mobilization is usually thought to be a post-germination process, seed reserve proteins mobilization occurs during germination. This study quantified seed proteins of bean genotypes during different hydration times, in order to understand the process of protein mobilization and whether there is relationship of this biochemical component with seed vigor. This study was conducted using seeds with different levels of vigor, genotypes with highest (13, 42, 55 and 81) and lowest (07, 23, 44, 50, IPR-88-Uirapurú and Iapar 81) physiological quality. High vigor genotypes showed greater efficiency in hydrolysis and mobilization of protein component, because they presented low globulins content in cotyledons at radicle protrusion in relation to low vigor genotypes (07, 23 and 50). The protein alpha-amylase inhibitor, observed in all genotypes, is involved with the longer time needed for radicle protrusion, according to the band intensity difference in genotypes 07, 44 and Iapar 81.

scholarly journals Polymorphism of buckwheat seed storage proteins in cultivar groups, differing by their morphotype

2019 ◽  
Vol 6 (1) ◽  
pp. 10-17
Author(s):  
Ye. Zaika ◽  
N. Kozub ◽  
I. Sozinov ◽  
G. Bidnyk ◽  
P. Karazhbey
Keyword(s):  
Genetic Markers ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Breeding Programs ◽  
Cultivar Groups

Aim. To study polymorphism of buckwheat seed proteins in cultivar groups of different morphotypes by the color of corolla. Methods. Electrophoresis by Laemmli method in 17.5 % separating PAAG gel. Results. Electrophoresis spectrum variants with the incidence from 1 to 76 %, common for buckwheat cultivar groups, which are different in their morphotype, were revealed. The obtained results demonstrate a particular level of heterogeneity by the revealed variants in each investigated group of buckwheat genotypes. Variants 2h and 4f, occurring with the incidence of 10 % and 8 % respectively, and specifi c for green-fl owered group of buckwheat cultivars, were also revealed. Conclusions. Different incidence of electrophoresis spectrum components in buckwheat morphotypes, different in fl ower coloring, demonstrates probable different selective value of genes, which control the synthesis of these components or their relation to the genes, closely bound to them. Taking this fact into consideration, buckwheat seed proteins may be molecular and genetic markers for identifi cation of some buckwheat morphotypes, which may be used in breeding programs.

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