Taxonomic significance of seed protein profiles in Acacia, with special reference to Acacia emilioana

2003 ◽  
Vol 16 (1) ◽  
pp. 35 ◽  
Author(s):  
Alicia L. Lamarque ◽  
Renée H. Fortunato
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
High Concentration ◽  
Protein Patterns ◽  
Qualitative And Quantitative ◽  
Sds Page ◽  
Electrophoretic Data ◽  
Main Protein ◽  
Protein Components ◽  
Total Seed

Total seed proteins of 10 Acacia species were examined by SDS–PAGE. The protein patterns showed qualitative and quantitative differences among the taxa analysed. The main protein components of most species examined had MW's in the range of 38.5–49.0 × 103. Subgenus Aculeiferum differed from subg. Acacia in the presence of a high concentration of proteins in the range of 20–24.5 × 103. Hierarchical clustering of the 10 taxa was undertaken, based on Jaccard distances calculated from electrophoretic data. The species grouped in two main clusters, representing the two subgenera of Acacia that occur in America, namely subg. Acacia and subg. Aculeiferum. The taxonomic placement of Acacia emilioana, a species with uncertain sectional affinity within subg. Aculeiferum, is discussed.

scholarly journals Seed protein variability in safflower

2002 ◽  
pp. 29-34
Author(s):  
Dragana Obreht ◽  
Ljiljana Vapa ◽  
Sándor Kis ◽  
Mária-Hajos Takács ◽  
Éva-Bányai Stefánovics ◽  
...  
Keyword(s):  
Protein Content ◽  
Seed Protein ◽  
Seed Proteins ◽  
Carthamus Tinctorius ◽  
Seed Protein Content ◽  
Electrophoretic Patterns ◽  
Sds Page ◽  
The Usa ◽  
Molecular Masses ◽  
Total Seed

Total seed proteins in two safflower species (Carthamus tinctorius L. and C. lanatus L) have been separated by the SDS-PAGE method. Their molecular masses ranged from 120 to 20 kDa. All C. tinctorius genotypes under study exhibited identical electrophoretic patterns which differed from the pattern exhibited by the wild species C. lanatus in the number and position of protein bands. Differences in protein profiles occurred in regions around 60 kDa, from 43 to 36 kDa and around 30 kDa. Statistically significant differences in seed protein content were found among safflower genotypes from different countries as well as among genotypes from the same country but from different sites. The highest seed protein content was found in a genotype originating from the USA.

scholarly journals Differences in tomato seed protein profiles obtained by SDS-PAGE analysis

2008 ◽  
Vol 53 (1) ◽  
pp. 13-23
Author(s):  
Elizabeta Miskoska-Milevska ◽  
Blagica Dimitrievska ◽  
Koo Poru ◽  
Zoran Popovski
Keyword(s):  
Seed Protein ◽  
Seed Proteins ◽  
Protein Profiles ◽  
Protein Fragment ◽  
Tomato Seed ◽  
Protein Fragments ◽  
Molecular Weights ◽  
Tomato Seeds ◽  
Sds Page ◽  
Total Seed

The protein profiles of tomato seeds from sub-species ( subsp. cultum Brezh., subsp. subspontaneum Brezh. and subsp. spontaneum Brezh.) were analyzed using SDS-PAGE technique. Electrophoreograms and denzitograms of total, soluble and non-soluble proteins of 31 different samples have showed quantitative and qualitative differences. Qualitative differences in electrophoregrams of total seed proteins refer to protein fragments in zone A (114 kDa, 83 kDa and 65 kDa) and protein fragment in zone C (17 kDa). Qualitative differences in electrophoregrams of soluble seed proteins refer to protein fragment in zone A (94 kDa). Qualitative differences in electrophoregrams of nonsoluble seed proteins refer to protein fragments with molecular weights of: 210 kDa, 85 kDa, 67 kDa and 26 kDa.

Electropherogram pattern similarity of seed proteins from 21 different soybean (Glycine max) varieties

1977 ◽  
Vol 55 (16) ◽  
pp. 2245-2250 ◽  
Author(s):  
Clifton F. Savoy
Keyword(s):  
Glycine Max ◽  
Seed Protein ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Plant Proteins ◽  
Relative Mobility ◽  
Molecular Weights ◽  
Pattern Similarity ◽  
Protein Components ◽  
Phosphate Detergent

Soybean (Glycine max) seed protein has been characterized using a phosphate-detergent (sodium dodecyl sulfate) polyacrylamide gel electrophoretic system, which has been extensively tested on plant proteins. The same general densitometer electropherogram pattern as regards numbers and kinds of protein components resolved was observed for all soybean varieties tested, and one pattern is presented along with appropriate descriptive characterizations (numbers, molecular weights, relative mobility, and light absorption at 597 nm) to aid in distinguishing the components. Quantitative differences, however, of individual components may occur.

The Electrophoretic Contribution to the Solutions of Taxonomical Problems of Some Lathyrus L. Taxa Growing in Turkey

2020 ◽  
Author(s):  
H. Genc ◽  
İ. Emre ◽  
A. Sahin
Keyword(s):  
Seed Storage Protein ◽  
Extraction Procedure ◽  
Seed Proteins ◽  
Seed Storage ◽  
Morphological Data ◽  
Protein Patterns ◽  
Documentation System ◽  
Natural Habitats ◽  
Protein Assay ◽  
Sds Page

Background: The seed proteins are used as molecular markers to clarify the systematic problems. Also, electrophoretic techniques are safe tools to identify the seed proteins. In present study, it was used the SDS-PAGE technique to solve the taxonomical problems of eight taxa of genus Lathyrus belong to three sections Orobus, Lathyrostylis and Pratensis according to the globulin B and glutelin. Methods: The seed materials were collected from natural habitats and 0.5 g seed were homogenized and centrifuged based on extraction procedure. In addition, the amounts of seed storage protein subfractions were determined by using protein assay. The electrophoretic analysis were performed according to the 12% SDS-PAGE. The gel documentation system (Bio-Rad, USA) was used to analyse the electrophoretic data and UPGAMA was used to construct the dendogram to show the relationships among the species under focus. Results: Current study showed that the species of section Pratensis were different from species of sections Orobus and Lathyrostylis. The differences among the studied taxa shown clearly and all studied taxa were choosen from the protein patterns. Furthermore, present study demonstrated that L. nivalis has the highest globulin B and glutelin. Results of the present study generally supported the morphological data.

Inter and Intra-Specific Variation in SDS-PAGE of Total Seed Protein in Rice (Oryza sativa L.) Germplasm

2004 ◽  
Vol 7 (2) ◽  
pp. 139-143 ◽  
Author(s):  
Rehana Asghar ◽  
Rabia Siddique . ◽  
Muhammad Afzal . ◽  
Shamim Akhtar .
Keyword(s):  
Oryza Sativa ◽  
Seed Protein ◽  
Oryza Sativa L ◽  
Sds Page ◽  
Specific Variation ◽  
Total Seed

scholarly journals Lectins from Pisum arvense seeds behave differently from storage proteins during germination in the darkness

2000 ◽  
Vol 12 (3) ◽  
pp. 255-262 ◽  
Author(s):  
LUIZA IZABEL M. MOREIRA DA SILVA ◽  
MÁRCIO VIANA RAMOS ◽  
JOÃO BATISTA CAJAZEIRAS ◽  
PATRÍCIA RODRIGUES FERREIRA ◽  
CARLOS ALBERTO V. CARVALHO ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Proteolytic Enzymes ◽  
Seed Proteins ◽  
High Molecular Mass ◽  
Mass Storage ◽  
Pisum Arvense ◽  
Germination Process ◽  
Sds Page ◽  
Haemagglutinating Activity ◽  
Main Protein

ABSTRACT - The mobilization of seed proteins from Pisum arvense L. during germination in the absence of light was studied. The seeds were found to be completely consumed 22 days after germination and seedlings ceased growth after the 18th day. SDS-PAGE indicated that the main protein bands correspond to high molecular mass storage proteins which undergo proteolysis in the initial stages of germination and are not detected after the 7th day of germination. However, the corresponding lectin profiles were detected during the entire germination process, suggesting that these proteins are strongly resistant to seed proteolytic enzymes and should be important for seedling establishment. Furthermore, haemagglutinating activity in cotyledons was detected until 22 days after germination, indicating that the lectins remain active even in senescent cotyledons.

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