Isolation and Composition of the Seed Globulins of Winged Bean, Psophocarpus tetragonolobus (L.) DC

1978 ◽  
Vol 5 (3) ◽  
pp. 357 ◽  
Author(s):  
JM Gillespie ◽  
RJ Blagrove
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Winged Bean ◽  
The Other ◽  
Bean Seed ◽  
Psophocarpus Tetragonolobus ◽  
Disulfide Bonding ◽  
Single Protein ◽  
Seed Globulins ◽  
Sulfur Containing

The amino acid composition of winged bean seed meal is similar to that of soybean but their storage globulins are quite different. Winged bean proteins are soluble to the extent of 60% at the pH of a meal-water slurry (pH 6.6), 80% at pH 11 but only 12% at pH 5. However, the proteins are soluble to the extent of 80% from pH 5 to 9 in 10% NaCl rising to 90% at pH 11. There are no satisfactory ways of recovering all the proteins from solution by simple changes in pH or ionic strength. Winged bean seed contains major proteins with sedimentation coefficients of 2 S and 6 S. Electrophoresis on cellulose acetate resolves three globulin fractions which we have named psophocarpins A, B, and C. The proteins from these electrophoretic regions have been isolated and partially purified. Psophocarpin A is essentially a single protein comparatively rich in sulfur-containing amino acids while the other fractions are composed of a number of related components which have not been separated. When examined by SDS-polyacrylamide gel electrophoresis, the globulin fractions differed in the kind of subunit proteins they contain and in the extent of disulfide bonding. The 40 000 mol. wt subunit of psophocarpin A contains disulfide bonded chains of mol. wt 16 000 and 24 000. The proteins corresponding to the other electrophoretic regions are more complex.

Variability of the Seed Globulins of Winged Bean, Psophocarpus tetragonolobus (L.) DC

1978 ◽  
Vol 5 (3) ◽  
pp. 371 ◽  
Author(s):  
RJ Blagrove ◽  
JM Gillespie
Keyword(s):  
Protein Content ◽  
Papua New Guinea ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Psophocarpus Tetragonolobus ◽  
Electrophoretic Patterns ◽  
Pure Lines ◽  
Seed Globulins ◽  
Single Subunit

Extracts from the seeds of 80 pure lines of P. tetragonolobus found in Papua New Guinea have been examined by polyacrylamide gel electrophoresis, There was little difference between the electrophoretic patterns except for variation in the proportion of one polypeptide. In its unreduced form, this polypeptide is the single subunit of psophocarpin A. A number of these genotypes have been studied more closely to obtain information regarding their protein content and the influence of extraction conditions on the protein pattern observed.

scholarly journals Studies on Platelet Glycoproteins by Surface Labeling and SDS Polyacrylamide Gel Electrophoresis

1977 ◽  
Author(s):  
I. Hagen ◽  
N.O. Solum ◽  
M. Peterka
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Conformational State ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Metabolic Inhibitors ◽  
Conventional System ◽  
Platelet Surface ◽  
Release Reaction

Platelet surface (glyco)proteins, and alterations in these in connection with the thrombin-induced release reaction has been studied. Platelets were labeled by lactoperoxidase-catalyzed iodination, and examined by SDS gel electrophoresis in two different gel systems, one conventional(J. Biol. Chem.1969 244 4406), and the other containing urea and EDTA in the gels. In the conventional system the bulk of radioactivity coincided with a PAS band (GP III) of MW about 100, 000. In the other system, the main radioactive peak appeared in the GP II area (MW 120,000), and a shift in the PAS stain intensity from GP III to GP II was seen. Thrombasthenic platelets showed only traces of the GP II band in both systems. The bulk of radioactivity was associated with the surface glycopolypeptide GPS, which is present, but not labeled in normal platelets. In thrombin-released platelets, GPS in its unreduced state has an altered electrophoretic mobility compared to control platelets and platelets which have been incubated with metabolic inhibitors to prevent secretion. The findings indicate that the GP III band consists of two different polypeptides, one of which appears in the GP II area in gels containing urea and EDTA. Further, that thrombasthenic platelet membrane exists in a conformational state different from that of normal platelets. And finally, GPS is in some way involved in, or influenced by, the thrombin-induced release reaction.

II. Mitt.: Auflösung der Chromoproteidfraktion aus Rattenleber-Ribosomen mit Hilfe der Polyacrylamidgel-Elektrophorese

1970 ◽  
Vol 25 (1) ◽  
pp. 67-72 ◽  
Author(s):  
Wolfram Domschke ◽  
Jürgen G. Meyer-Bertenrath
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
The Other ◽  
Blue Staining ◽  
Ribosomal Subunits ◽  
Molecular Weights ◽  
The One ◽  
Liver Ribosomes

After preparation of a coloured protein component containing iron from rat liver ribosomes 1 this fraction was submitted to detailed analysis by means of polyacrylamide gel electrophoresis. Thus it may be separated into one main and two secondary bands, which do not contain RNA detectable by methylene blue staining. The ferric content of all bands can be demonstrated by staining with 2,4-dinitroso-1,3-naphthalenediol 2. These bands are to be found in the large ribosomal subunits as well as in the small one in qualitative conformity, they differ, however, in their quantitative relations to each other depending on origin. LiCl-extraction as described for the preparation of ribosomal proteins causes dissociation of the chromoproteid fraction into six bands possessing lower molecular weights each than the original bands.The chromoproteids, localized in the large ribosomal subunits on the one hand and in the small subunits on the other hand were prepared differentiatedly by gel filtration. Results show the chromoproteid represented in the 57-S-subunit on a bigger scale than the nucleoproteid part, on the contrary, the 29-S-subunit is constructed of RNA-containing material preferably.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

Inheritance and linkage relationships of seed peroxidase loci in hexaploid oat (Avena sativa L.)

Genome ◽  
1995 ◽  
Vol 38 (3) ◽  
pp. 467-471
Author(s):  
N. R. Sharopova ◽  
A. A. Sozinov ◽  
V. A. Portyanko
Keyword(s):  
Avena Sativa ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Linkage Groups ◽  
Peroxidase Isozyme ◽  
Linkage Relationships

Polyacrylamide gel electrophoresis has been used to investigate the inheritance and linkage relationships between anodal (PXA) and cathodal (PXC) seed peroxidases in hexaploid oat (Avena sativa L.). A total of 12 seed peroxidase loci (5 loci of PXA and 7 loci of PXC) were identified in three crosses. Only two Pxc loci (Pxc5 and Pxc7) were not linked to any peroxidase loci; the others were scored in three linkage groups. The order of the three loci assigned to one of the linkage groups was Pxc1–Pxa5–Pxc2. The order of loci in the other two linkages were Pxc4–Pxa1–Pxa3 and Pxc3–Pxa4–Pxa2. Also, the Pxc6 locus was shown to be linked to the Pxc3 locus. Considering that A. sativa is an allohexaploid, it can be proposed that the three peroxidase linkages represent homoeologous chromosomes.Key words: seed peroxidase, isozyme inheritance, linkage, Avena sativa.

scholarly journals Phytoferritin is synthesized in vitro as a high-molecular-weight precursor. Studies on the synthesis and the uptake in vitro of the precursors of ferritin and ferredoxin by intact chloroplasts

1983 ◽  
Vol 214 (3) ◽  
pp. 943-950 ◽  
Author(s):  
F van der Mark ◽  
W van den Briel ◽  
H G Huisman
Keyword(s):  
Gel Electrophoresis ◽  
Biosynthetic Pathway ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
French Bean ◽  
Polyacrylamide Gel ◽  
Cell Organelle ◽  
Bean Seed ◽  
Intact Chloroplasts

Evidence is presented that French-bean (Phaseolus vulgaris) seed ferritin is composed of one type of subunit with an apparent Mr of 26500. In normal and iron-loaded leaf tissues it is detected immunologically with an antiserum raised against purified bean seed ferritin and migrates in SDS (sodium dodecyl sulphate)/polyacrylamide-gel electrophoresis with the same mobility as the bean seed ferritin subunit. The biosynthetic pathway of ferritin in normal and iron-loaded leaves was investigated. RNA was extracted, fractionated into polyadenylated RNA and translated in a cell-free rabbit reticulocyte lysate and a wheat-germ-extract system. The products were identified by SDS/polyacrylamide-gel electrophoresis after indirect immunoprecipitation. In all cases the ferritin product had an Mr 5000 higher than that of the native subunit. Uptake and processing of the precursor form of ferritin from iron-loaded leaves by intact chloroplasts was demonstrated. This indicates that, in iron-loaded leaves, ferritin acts as a chloroplast protein. We propose that the ferritin precursor in normal leaves follows the same biosynthetic pathway. This suggests that the iron-buffering function of ferritin in plants takes place in the chloroplast and that non-functional cellular iron will accumulate in this cell organelle.

scholarly journals New Exfoliative Toxin Produced by a Plasmid-Carrying Strain of Staphylococcus hyicus

1999 ◽  
Vol 67 (8) ◽  
pp. 4014-4018 ◽  
Author(s):  
Hisaaki Sato ◽  
Takao Watanabe ◽  
Yasuko Murata ◽  
Ayumi Ohtake ◽  
Mayumi Nakamura ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Staphylococcus Aureus ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
The Other ◽  
Exfoliative Toxin ◽  
Sds Page ◽  
Serotype B

ABSTRACT A new serotype of Staphylococcus hyicus exfoliative toxin (SHET), serotype B, was isolated from the culture filtrate of a plasmid-carrying strain of S. hyicus. The new SHET was purified by precipitation with 70% saturated ammonium sulfate, gel filtration on a Sephadex G-75 column, column chromatography on DEAE–Cellulofine A-500, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The new SHET caused exfoliation of the epidermis as determined by the so-called Nikolsky sign when inoculated into 1-day-old chickens. The new SHET was serologically different fromStaphylococcus aureus exfoliative toxins (ETs) (ETA, ETB, and ETC) and from the SHET from the plasmidless strain but showed the same molecular weight as the other serotypes of toxins on SDS-PAGE. It was thermolabile and lost its toxicity after being heated at 60°C for 30 min. We propose that the new SHET be designated SHETB and that the SHET produced by the plasmidless strain be designated SHETA.

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