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.

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 Extraction and Characterization of “Batuan” [Garcinia binucao (Blco.) Choisy] Seed Protein

2014 ◽  
pp. 89-103 ◽  
Author(s):  
Elizabeth Quevedo ◽  
Marivic Lacsamana ◽  
Antonio Laurena
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Seed Protein ◽  
Seed Proteins ◽  
Essential Amino Acids ◽  
Food Supplement ◽  
Seed Meal ◽  
Molecular Weights ◽  
Hydrophobic Amino Acids ◽  
Amino Acid Score

“Batuan” [Garcinia binucao (Blco.) Choisy], an indigenous, lesser known member of the Gutifferae family with export potential is underutilized and understudied. The present study was carried out to extract and characterize the protein in “batuan” [Garcinia binucao (Blco.) Choisy] seeds for nutritional quality assessment. Protein content of “batuan” seed meal was 8.9 ± 0.59% dry basis. Solubility fractionation of “batuan” seed meal showed globulin and glutelin as the major seed proteins. SDS-PAGE resolved the globulin and glutelin into three groups of polypeptides with molecular weights of about 20 – 54 kDa. Amino acid analysis revealed that seed protein contained all the essential amino acids with leucine as the most abundant while tryptophan, the least. “Batuan” seed proteins were mostly made up of acidic and hydrophobic amino acids with glutamic acid (2.67%) as the highest. Nutritional assessments including E/T (38.4%), amino acid score (1.6%), predicted PER (3.2-3.7) and estimated BV (98.3%) suggested that the seed proteins are of good quality. Hence, “batuan” seeds has a promising potential as an important sources of valuable proteins and amino acids for use as food supplement/enhancing ingredient.

scholarly journals Polyacrylamide gel electrophoresis of soybean seed proteins

2015 ◽  
Vol 47 (4) ◽  
pp. 371-378 ◽  
Author(s):  
W. Lassocińsk ◽  
J. S. Knypl
Keyword(s):  
Glycine Max ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Soybean Seed ◽  
Seed Proteins ◽  
Soluble Proteins ◽  
Polyacrylamide Gel ◽  
Major Protein ◽  
Molecular Weights ◽  
Minor Protein

Four major and 14 minor protein bands were detected when total salt soluble proteins of soybean (Glycine max cultivar Warszawska) seed were subjected to polyacrylamide gel electrophoresis under nondissociating conditions, and 16 protein bands were detected under dissociating conditions. Molecular weights of three major protein fractions in PAGE SDS were determined for around 18 500, 36 000 and 80 000 daltons.

scholarly journals Purification and characterization of two components of botulinum C2 toxin

1980 ◽  
Vol 30 (3) ◽  
pp. 668-673
Author(s):  
I Ohishi ◽  
M Iwasaki ◽  
G Sakaguchi
Keyword(s):  
Sodium Dodecyl ◽  
Molecular Characteristics ◽  
Homogeneous State ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Separate Protein ◽  
Protein Components ◽  
C2 Toxin ◽  
Lethal Doses

Two dissimilar proteins, designated as components I and II, of botulinum C2 toxin elaborated by strain 92-13 were purified to a homogeneous state. The molecular weights determined by sodium dodecyl sulfate gel electrophoresis were 55,000 for component I and 105,000 for component II. Whereas each component showed no or feeble toxicity even after being treated with trypsin, the toxicity was elicited when these two components were mixed and trypsinized. The toxicity of the mixture of components I and II at a ratio of 1:2.5 on a protein basis was 2.2 X 10(4) mouse intraperitoneal 50% lethal doses per mg of protein and increased by 2,000 times or more when treated with trypsin. These results indicate that the molecular characteristics of botulinum C2 toxin differ from those of the toxin of Clostridium botulinum types A through F in that C2 toxin is constructed with two separate protein components, which are not covalently held together, and that its toxicity is elicited by cooperation of the two components.

Studies on the Stellaria longipes complex (Caryophyllaceae). VII. The seed proteins

1986 ◽  
Vol 64 (7) ◽  
pp. 1327-1330 ◽  
Author(s):  
David J. Gifford ◽  
C. C. Chinnappa
Keyword(s):  
Species Complex ◽  
Polyacrylamide Gel Electrophoresis ◽  
General Pattern ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Distinct Species ◽  
Major Protein ◽  
Stellaria Longipes ◽  
Cytogenetic Studies ◽  
Protein Components

Seed proteins of Stellaria longipes s.l. 2n = 52, 78, and 104, have been characterized using sodium dodecyl sulphate – polyacrylamide gel electrophoresis. The same general pattern as regards the number of major protein components resolved was observed in all the genotypes and cytotypes studied. These included all the morphotypes that were described as distinct species. The present data do not contradict the conclusions drawn from cytogenetic studies that all the morphological types are closely related and are part of a polyploid species complex.

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.

scholarly journals Microfibrillar Proteins of Wool: Partial Specific Volumes and Molecular Weights in Denaturing Solvents

1979 ◽  
Vol 32 (5) ◽  
pp. 423 ◽  
Author(s):  
EF Woods
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Guanidine Hydrochloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Equilibrium ◽  
Molecular Weights ◽  
Dodecyl Sulfate ◽  
Protein Components ◽  
Wool Proteins ◽  
Specific Volumes

The molecular weights of the reduced and S-carboxymethylated microfibrillar protein components of wool have been investigated by sedimentation equilibrium in 6 M guanidine hydrochloride and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The microfibrillar proteins have molecular weights of 57000 (component 5), 58000 (component 7c); 50000 (component 8c-l) with a range of values for the other component 8 polypeptide chains of 45 000--50 000. The proteins migrate anomalously in polyacrylamide gels in the presence of sodium dodecyl sulfate as seen from a comparison of the free mobilities and retardation coefficients of standard proteins with those of the wool proteins. More reliable molecular weights were obtained by plotting the retardation coefficients against molecular weights (Ferguson plot). The partial specific volumes of the microfibrillar proteins have been measured in dilute aqueous buffer solutions, 8 M urea and 6 M guanidine hydrochloride. The values are compared to those calculated from the amino acid compositions.

Electron Microscope Study of RNA's of Paramyxoviruses

1972 ◽  
Vol 30 ◽  
pp. 196-197
Author(s):  
Ruchama Baum ◽  
J.T. Seto
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Electron Microscope Study ◽  
Sendai Virus ◽  
Sodium Dodecyl ◽  
Rna Molecules ◽  
Virus Particles ◽  
Molecular Weights ◽  
Length Measurements

The ribonucleic acid (RNA) of paramyxoviruses has been characterized by biochemical and physiochemical methods. However, paramyxovirus RNA molecules have not been studied by electron microscopy. The molecular weights of these single-stranded viral RNA molecules are not known as yet. Since electron microscopy has been found to be useful for the characterization of single-stranded RNA, this investigation was initiated to examine the morphology and length measurements of paramyxovirus RNA's.Sendai virus Z strain and Newcastle disease virus (NDV), Milano strain, were used. For these studies it was necessary to develop a method of extracting RNA molecules from purified virus particles. Highly purified Sendai virus was treated with pronase (300 μg/ml) at 37°C for 30 minutes and the RNA extracted by the sodium dodecyl sulfate (SDS)-phenol procedure.

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

GENETIC DIVERSITY IN BAMBARA GROUNDNUT (Vigna subterranean) AS REVEALED BY MOLECULAR WEIGHTS OF THE SEEDS’ PROTEINS

2018 ◽  
Vol 30 (2) ◽  
pp. 19-28
Author(s):  
A. J. Oludare ◽  
J. I. Kioko ◽  
A. A. Akeem ◽  
A. T. Olumide ◽  
K. R. Justina ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Seed Proteins ◽  
Electrophoretic Analysis ◽  
Protein Characterization ◽  
Bambara Groundnut ◽  
Vigna Subterranea ◽  
Phylogenetic Relatedness ◽  
Molecular Weights ◽  
National Centre ◽  
Standard Marker

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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