COMPARISON OF GLIADIN AND GLUTENIN SUBUNITS IN THE TRITICINAE BY SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS

1975 ◽  
Vol 55 (3) ◽  
pp. 667-672 ◽  
Author(s):  
K. R. PRESTON ◽  
W. WOODBURY ◽  
R. A. ORTH ◽  
W. BUSHUK
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel ◽  
Glutenin Subunits ◽  
Protein Subunits ◽  
Molecular Weights ◽  
Aegilops Squarrosa ◽  
Secale Cereale L

Protein subunits obtained by reduction of gliadin and glutenin from Triticum aestivum L. em. Thell. (AABBDD), Triticum monococcum L. (AA), Aegilops squarrosa L. (DD) and Secale cereale L. (RR) were examined by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Seven of the twelve gliadin subunits and nine of the fifteen glutenin subunits present in T. aestivum had molecular weights (MW’s) similar to subunits present in both T. monococcum and A. squarrosa. An additional five gliadin and five glutenin subunits present in T. aestivum had MW’s similar to subunits present in T. monococcum or A. squarrosa. S. cereale had a lower number of gliadin and glutenin subunits. However, three of four gliadin subunits and eight of nine glutenin subunits had MW’s similar to subunits present in the Triticum–Aegilops groups. These results have been used to consider evolutionary relationships in the Triticinae.

Structural polypeptides of cholera bacteriophage

1981 ◽  
Vol 27 (1) ◽  
pp. 72-75 ◽  
Author(s):  
K. Chaudhuri ◽  
M. Maiti
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Total Protein ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Weights

The structural polypeptides of the cholera bacteriophage [Formula: see text] have been analysed by sodium dodecyl sulphate – polyacrylamide gel electrophoresis. Eight different polypeptides were identified. The apparent molecular weights of the polypeptides were 143 000, 96 500, 68 000, 53 000, 37 500, 29 500, 21 000, and 13 500, respectively. The percentage of total protein corresponding to each polypeptide was estimated.

scholarly journals Purification and subunit structure of legumin of Vicia faba L. (broad bean)

1974 ◽  
Vol 141 (2) ◽  
pp. 413-418 ◽  
Author(s):  
David J. Wright ◽  
Donald Boulter
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Broad Bean ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Polyacrylamide Gel ◽  
Subunit Structure ◽  
Isoelectric Precipitation ◽  
Molecular Weights

Zonal isoelectric precipitation was shown to be an effective method for the preparation of legumin which was homogeneous as judged by ultracentrifugation and polyacrylamide-gel electrophoresis. The subunit structure of legumin was investigated by preparative sodium dodecyl sulphate–polyacrylamide-gel electrophoresis and ion-exchange chromatography in urea. Five distinct subunits, of which two were acidic (α) and had a molecular weight of 37000, and three were basic (β) with molecular weights of 20100, 20900 and 23800, were identified. The α and β subunits were present in equimolar amounts in the legumin molecule and, in view of this and molecular-weight considerations, an α6β6 subunit model was proposed for legumin.

ISOLATION OF LH, FSH AND TSH FROM HUMAN PITUITARIES AFTER THE REMOVAL OF HGH

1974 ◽  
Vol 77 (3) ◽  
pp. 485-497 ◽  
Author(s):  
P. A. Torjesen ◽  
T. Sand ◽  
N. Norman ◽  
O. Trygstad ◽  
I. Foss
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Disc Electrophoresis ◽  
Exchange Chromatography ◽  
Polyacrylamide Gel ◽  
Molecular Weights ◽  
Pituitary Glands

ABSTRACT Highly purified human LH, FSH and TSH were isolated from batches of 300 frozen pituitary glands (200 g) by pH, acetone and ethanol fractionation, Sephadex gel filtration, ion-exchange chromatography on DEAE-cellulose and CM-Sephadex, and preparative polyacrylamide-gel electrophoresis. Sodium dodecyl-sulphate (SDS) polyacrylamide gel electrophoresis was used in order to check the purity, the identity and the molecular weight of the purified LH, FSH and TSH. This procedure showed that the hormone preparations consisted of two subunits with molecular weights of: LH: 21 300 and 17 900, FSH: 22 100 and 18 300 and TSH: 20 800 and 16 400. The purity of the hormone preparations was also evaluated by analytical disc electrophoresis at pH 8.9. The purified hormone preparations had radioimmunological activity as follows: LH: 20 000 IU/mg, FSH: 16 500 IU/mg and TSH: 5 IU/mg. All preparations had high biological potency.

Isoelectric points and molecular weights of salt-extractable ribosomal proteins

1976 ◽  
Vol 54 (12) ◽  
pp. 1029-1033 ◽  
Author(s):  
M Saleem ◽  
Burr Atkinson
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Acidic Proteins ◽  
Gel Isoelectric Focusing ◽  
Liver Ribosomes

Rat liver ribosomes prepared in low salt buffer contain basic and acidic proteins not found on ribosomes washed in high salt buffer. Proteins extracted from liver ribosomes by 500 mM KCl were characterized by acid urea–polyacrylamide gel electrophoresis, sodium dodecyl sulfate – polyacrylamide gel electrophoresis and gel isoelectric focusing. The salt-solubilized proteins contain 12 polypeptides with a molecular weight over 67 000, several polypeptides with molecular weights less than 67 000, and three polypeptides whose molecular weight exceeded 130 000. Ten to 12 of the proteins were basic, and about 24 acidic proteins were partially or wholly extracted from the ribosomes. Four of the acidic proteins have isoelectric points less than 4.5.

Diversity of seed storage proteins in common wheat (Triticum aestivum L.)

2011 ◽  
Vol 9 (2) ◽  
pp. 256-259
Author(s):  
Zuzana Šramková ◽  
Edita Gregová ◽  
Svetlana Šliková ◽  
Ernest Šturdík
Keyword(s):  
Triticum Aestivum ◽  
Common Wheat ◽  
Gel Electrophoresis ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel

The objective of our study was to determine the composition of high-molecular weight-glutenin subunits (HMW-GS) in 120 cultivars of common wheat (Triticum aestivum L.). Fourteen alleles and 34 allelic compositions were detected using sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The most frequent HMW-GS alleles at the Glu-A1, Glu-B1 and Glu-D1 loci were null (57.1%), 7+9 (43.3%) and 5+10 (61.9%), respectively. However, low-frequency HMW-GS alleles were also observed, such as 13+16, 20, 21, 7 and 18, encoded by the Glu-B1 locus, and 4+12, encoded by the Glu-D1 locus. The wheat–rye 1BL.1RS translocation was identified in 25 cultivars, using acid polyacrylamide gel electrophoresis. The Glu-score varied greatly, and some lines reached the maximum value of 10.

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