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.

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.

IDENTIFICATION OF CULTIVARS OF FORAGE LEGUME (Desmodium ovalifolium GUILL ET PERR.) BY THEIR ELECTROPHORETIC PATTERNS

1987 ◽  
Vol 67 (3) ◽  
pp. 713-717 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
H. RAMIREZ ◽  
W. ROCA
Keyword(s):  
Gel Electrophoresis ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legume ◽  
Desmodium Ovalifolium ◽  
Electrophoretic Patterns ◽  
Electrophoretic Procedure

An electrophoretic procedure was developed for discriminating cultivars of Desmodium ovalifolium on the basis of patterns of partially purified seed proteins. Electrophoresis was done on uniform 15% polycrylamide gels in basic (8.9) pH. The method produced satisfactory discrimination of eight cultivars used in its initial evaluation.Key words: Forage legume, Desmodium ovalifolium Guill et Perr., cultivar identification, polyacrylamide gel electrophoresis

scholarly journals Analysis of Several Popular Cultivars of Madagascar Periwinkle (Catharanthus roseus (L.) G. Don.) using Biochemical Markers

2013 ◽  
Vol 5 (4) ◽  
pp. 458-461
Author(s):  
Owk ANIEL KUMAR ◽  
Sape S. TATA ◽  
Kancharla PAVAN KUMAR
Keyword(s):  
Catharanthus Roseus ◽  
Gel Electrophoresis ◽  
Biochemical Markers ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cultivar Differences ◽  
Madagascar Periwinkle ◽  
Large White ◽  
Electrophoretic Patterns ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Isozyme Polymorphism

Band designs of esterase (EST), peroxidase (PO) and polyphenol oxidase (PPO) isozymes in several selected cultivars of Catharanthus roseus by using native polyacrylamide gel electrophoresis (PAGE) were investigated in this study. It was confirmed that cultivar differences in isozyme polymorphism can be revealed by applied electrophoretic patterns. Three isozyme systems produced a total of 16 bands with polymorphism ranged from 66.6-100%. Considering the patterns of isozyme variations in the five cultivars of Catharanthus roseus, it is evident that the cultivar ‘First kiss coral’ displayed crimson red petal with large white eye’ displayed demarked profiles of EST, PO and PPO isozymes than other cultivars. This is the first report on isozyme polymorphism in members of the Cathanarathus roseus (L.) G. Don.

scholarly journals Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresis

1970 ◽  
Vol 118 (2) ◽  
pp. 303-310 ◽  
Author(s):  
H. Winkler ◽  
Heide Hörtnagl ◽  
H. Hörtnagl ◽  
A. D. Smith
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Chromaffin Granules ◽  
Ph Optimum ◽  
Electrophoretic Patterns ◽  
Granule Membrane ◽  
Adrenal Chromaffin ◽  
Protein Treatment ◽  
Nucleoside Triphosphatase

Washed membranes of bovine adrenal chromaffin granules contained most of the cholesterol and phospholipids of the particle and 22% of the total protein. The protein/lipid ratio was about 0.45 (w/w). Dopamine(3,4-dihydroxyphenethylamine)β-hydroxylase, Mg2+-activated nucleoside triphosphatase and cytochrome b-559 activities were present in the membrane. ATP was the best substrate for the nucleoside triphosphatase, whose pH optimum was 6.4, Km 7×10−4m and Vmax. 1.8μmol/h per mg of protein. Treatment of the membranes with various detergents caused a preferential solubilization of protein compared with lipids. Membranes dissolved in sodium dodecyl sulphate or phenol–acetic acid–urea were subjected to polyacrylamide-gel electrophoresis at alkaline and acid pH respectively. The electrophoretic patterns given by the proteins of the chromaffin granule membrane were distinct from those given by the chromogranins, and from those given by mitochondrial and microsomal membrane proteins.

Electrophoretic and electron microscopic examination of the adductor and diductor muscles of an articulate brachiopod, Terebratalia transversa

1982 ◽  
Vol 60 (4) ◽  
pp. 550-559 ◽  
Author(s):  
William P. Eshleman ◽  
Jerrel L. Wilkens ◽  
Michael J. Cavey
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electron Microscopic Examination ◽  
Light Chains ◽  
Electron Microscopic ◽  
Electrophoretic Patterns ◽  
Transmission Electron ◽  
Adductor Muscles ◽  
Regulation Of Contraction

The proteins of the striated adductor muscles, smooth adductor muscles, and diductor muscles of the articulate brachiopod Terebratalia transversa have been examined by sodium dodecyl sulfate – polyacrylamide gel electrophoresis. Electrophoretic patterns indicate the presence of paramyosin in all of these valve muscles. Tentative identification has also been made of the proteins responsible for actin and for myosin regulation of contraction (troponin–tropomyosin and myosin light chains, respectively). The myofilaments of the striated adductor cells, smooth adductor cells, and diductor cells have been characterized by transmission electron microscopy. The smooth adductor cells and the diductor cells exhibit very thick myofilaments which are fusiform in shape, exceptionally long, and axially banded. Morphological features of these thick myofilaments are consistent with those of paramyosin filaments found in other muscles and myoepithelia. Although the striated adductor cells contain paramyosin, it is not manifest in the thick myofilaments.

Polyacrylamide gel electrophoresis and infrared spectroscopy of vibrio biotypes

1981 ◽  
Vol 27 (10) ◽  
pp. 1048-1052 ◽  
Author(s):  
M. Maiti ◽  
P. Sur ◽  
S. N. Chatterjee
Keyword(s):  
Infrared Spectroscopy ◽  
Vibrio Cholerae ◽  
Infrared Spectra ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Electrophoretic Patterns ◽  
Different Strains ◽  
El Tor

Polyacrylamide gel electrophoresis and infrared spectroscopy were used to study the relationship between Vibrio cholerae (classical), Vibrio cholerae (El Tor), and nonagglutinable (NAG) vibrios. Acid extracts of the different strains produced type-specific electrophoretic patterns, and the infrared spectra revealed broad absorption maxima which largely correspond to those found in other organisms. With the exception of the NAG vibrios, the infrared spectra of cholera El Tor vibrios were identical. Strain-specific differences were found in the exoprotein spectra of these organisms by the sodium dodecyl sulphate – polyacrylamide gel electrophoretic technique.

Changes of Antioxidant Enzyme and Phenylalanine Ammonia-Lyase Activities during Chimonanthus praecox Seed Maturation

2008 ◽  
Vol 63 (7-8) ◽  
pp. 569-573 ◽  
Author(s):  
Xiaojia He ◽  
Shun Gao
Keyword(s):  
Superoxide Dismutase ◽  
Protein Content ◽  
Antioxidant Enzyme ◽  
Gel Electrophoresis ◽  
Growth And Development ◽  
Phenylalanine Ammonia Lyase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Maturation ◽  
Pal Activity ◽  
Chimonanthus Praecox

Changes in peroxidase (POD), superoxide dismutase (SOD), catalase (CAT) and phenylalanine ammonia-lyase (PAL) activities were studied during Chimonanthus praecox seed maturation. According to our findings the protein content increased steadily from 8 to 12 weeks after flowering, and thereafter decreased significantly. Similarly, SOD and POD activities increased gradually up to 12 weeks after flowering and then declined. PAL activity declined gradually during seed maturation. CAT activity, however, showed no changes during seed maturation. By means of polyacrylamide gel electrophoresis (PAGE), SOD and POD isoenzymes were observed during seed maturation. The staining intensities of SOD and POD isoenzymes correlated well with SOD and POD activities as obtained by an assay in solution. These findings suggest that POD, SOD and PAL may be involved in the growth and development during Chimonanthus praecox seed maturation.

scholarly journals Alterations in Protein Expression Caused by thehha Mutation in Escherichia coli: Influence of Growth Medium Osmolarity

1999 ◽  
Vol 181 (10) ◽  
pp. 3018-3024 ◽  
Author(s):  
Carlos Balsalobre ◽  
Jörgen Johansson ◽  
Bernt Eric Uhlin ◽  
Antonio Juárez ◽  
Francisco J. Muñoa
Keyword(s):  
Escherichia Coli ◽  
Growth Medium ◽  
Gel Electrophoresis ◽  
Catabolite Repression ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Wild Type ◽  
Phosphotransferase System ◽  
New Family ◽  
Medium Osmolarity

ABSTRACT The Hha protein belongs to a new family of regulators involved in the environmental regulation of virulence factors. The aim of this work was to study the effect of the hha mutation on the overall protein pattern of Escherichia coli cells by two-dimensional polyacrylamide gel electrophoresis. The growth medium osmolarity clearly influenced the effect of the hhamutation. The number of proteins whose expression was altered inhha cells, compared with wild-type cells, was three times larger at a high osmolarity than at a low osmolarity. Among the proteins whose expression was modified by the hha allele, both OmpA and protein IIAGlc of the phosphotransferase system could be identified. As this latter enzyme participates in the regulation of the synthesis of cyclic AMP and hence influences the catabolite repression system, we tested whether the expression of thelacZ gene was also modified in hha mutants. This was the case, suggesting that at least some of the pleiotropic effects of the hha mutation could be caused by its effect on the catabolite repression system.

INFLUENCE OF SOURCE OF WHEAT CYTOPLASM ON THE NATURE OF PROTEINS IN HEXAPLOID TRITICALE

1974 ◽  
Vol 16 (3) ◽  
pp. 529-537 ◽  
Author(s):  
S. L. K. Hsam ◽  
E. N. Larter
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Proteins ◽  
Triticum Aestivum L ◽  
The Other ◽  
Hexaploid Triticale ◽  
Electrophoretic Patterns ◽  
High Molecular Weight Proteins

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to study seed proteins in 4 pairs of reciprocal F1 isogenic hybrids of hexaploid triticales differing only in their source of cytoplasm. One member of each reciprocal pair possessed the cytoplasm of hexaploid (6x) wheat (Triticum aestivum L. em. Thell), the other, the cytoplasm from tetraploid (4x) wheat (T. turgidum L). Qualitative as well as quantitative differences were observed in the electrophoretic patterns of the albumins and globulins. High molecular weight proteins (> 34,000 daltons) were synthesized in triticale with 6x wheat cytoplasm in greater quantity than in triticale with 4x wheat cytoplasm. Differences in the patterns of gliadin and reduced glutenin of the reciprocal triticale populations were quantitative. The relevance of these findings to seed development in triticales is discussed.

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