IDENTIFICATION OF CICER MILKVETCH CULTIVARS USING SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS

1983 ◽  
Vol 63 (4) ◽  
pp. 1087-1090 ◽  
Author(s):  
ROBERT K. EVANS ◽  
ROLLIN H. ABERNETHY
Keyword(s):  
Banding Pattern ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel ◽  
Forage Legumes ◽  
Electrophoretic Method ◽  
Stand Establishment ◽  
Astragalus Cicer ◽  
Varietal Purity

With the release of Monarch cicer milkvetch (Astragalus cicer L.), which has greatly facilitated stand establishment when compared to older cultivars, the desirability of a method for identifying seed of cultivars was recognized. An SDS-polyacrylamide gel electrophoretic method was developed to differentiate cicer milkvetch cultivars. Densitometric scanning of the resultant polypeptide banding pattern on the polyacrylamide gel provided identification of seed lots of the cultivars Oxley, Lutana and Monarch produced in several different years and locations.Key words: Astragalus cicer L., forage legumes, seed proteins, varietal purity

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 Purification and properties of β-mannanases I and II from the germinated seeds of Trifolium repens. Mode of galactomannan degradation in vitro

1978 ◽  
Vol 175 (3) ◽  
pp. 1079-1087 ◽  
Author(s):  
H Villarroya ◽  
J Williams ◽  
P Dey ◽  
S Villarroya ◽  
F Petek
Keyword(s):  
Trifolium Repens ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Ph Optimum ◽  
Electrophoretic Method ◽  
Germinated Seeds

Two beta-mannanases (beta-mannosidases, EC 3.2.1.25) purified from the germinated seeds of Trifolium repens by a procedure that included chromatography on hydroxyapatite, gel filtration on acrylamide/agarose (Ultragel 5/4) and preparative polyacrylamide-gel-electrophoresis. The final purification step completely resolved two beta-mannanases with distinct specificities, which were termed beta-mannanase I and beta-mannanase II. beta-Mannanase I was purified 1400-fold and beta-mannanase II 1000-fold. The purified enzymes showed a single protein band when examined by polyacrylamide-gel disc electrophoresis. beta-Mannanase I, apparent mol.wt. 43 000, accounted for 49% of the total activity recovered from the final step of purification. beta-Mannanase II, apparent mol.wt. 38 000, accounted for the remaining 51% of activity. Molecular-weight determinations were by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and by the electrophoretic method of Hendrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164]. The substrate specificities of both enzymes were examined with the galactomannans of T. repens and of Medicago sativa, as well as with manno-oligosaccharides. The pH optimum was between pH 5.1 and 5.6 for both enzymes.

DISCRIMINATION OF CULTIVARS OF LENTIL (Lens culinaris Medic.) BY ELECTROPHORESIS OF SEED PROTEINS

1989 ◽  
Vol 69 (1) ◽  
pp. 243-246 ◽  
Author(s):  
A. HUSSAIN ◽  
W. BUSHUK ◽  
K. W. CLARK
Keyword(s):  
Gel Electrophoresis ◽  
Lens Culinaris ◽  
Seed Protein ◽  
Cultivar Identification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Seed Proteins ◽  
Polyacrylamide Gel

Discrimination of lentil cultivars was achieved by analysis of seed protein by two types of polyacrylamide gel electrophoresis. Cultivars of lentil were discriminated by the presence or absence of diagnostic bands. Electrophoregrams of six seed lots of the cultivar Eston were identical and unaffected by growing conditions.Key words: Lens culinaris Medic, seed proteins, polyacrylamide gel electrophoresis, cultivar identification

scholarly journals Glycosidases induced in Aspergillus tamarii. Secreted α-d-galactosidase and β-d-mannanase

1984 ◽  
Vol 219 (3) ◽  
pp. 857-863 ◽  
Author(s):  
A Civas ◽  
R Eberhard ◽  
P Le Dizet ◽  
F Petek
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Preceding Paper ◽  
Protein Band ◽  
Polyacrylamide Gel ◽  
Aspergillus Tamarii ◽  
Electrophoretic Method ◽  
Single Protein

An alpha-D-galactosidase (EC 3.2.1.22) and a beta-D-mannanase (EC 3.2.1.78), which were secreted into the growth medium when Aspergillus tamarii was cultivated in the presence of galactomannan, were purified by a procedure including chromatography on hydroxyapatite and DEAE-cellulose columns. Each of these enzymes showed a single protein band, corresponding to their respective activities, on polyacrylamide-gel electrophoresis. Both enzymes were shown to be glycoproteins containing N-acetylglucosamine, mannose and galactose, with molar proportions of 1:6:1.5 for alpha-D-galactosidase and 1:13:8 for beta-D-mannanase. Mr values as determined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate and by the electrophoretic method of Hedrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164] were 56000 and 53000 respectively. The alpha-D-galactosidase differed markedly from the mycelial forms I and II studied in the preceding paper [Civas, Eberhard, Le Dizet & Petek (1984) Biochem. J. 219, 849-855] with regard to both its kinetic and structural properties.

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.

Polyacrylamide-Gel Disc-Electrophoresis as a Screening Procedure for Serum Lipoprotein Abnormalities

1973 ◽  
Vol 19 (2) ◽  
pp. 228-234 ◽  
Author(s):  
Herbert K Naito ◽  
Mitsuo Wada ◽  
L A Ehrhart ◽  
Lena A Lewis
Keyword(s):  
Gel Electrophoresis ◽  
Analytical Ultracentrifugation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Screening Method ◽  
Serum Lipoprotein ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Electrophoretic Method ◽  
Wide Range ◽  
Electrophoresis System

Abstract A polyacrylamide-gel disc-electrophoresis system is described that is suitable for screening sera with a wide range of lipid concentrations, and the results agree with analytical ultracentrifugation data. The lipoprotein pattern so obtained was compared with that obtained by other recognized electrophoretic procedures. Lipoprotein determinations were done by polyacrylamide gel electrophoresis, for 125 patients, to determine its merit as a clinical screening method for lipoprotein abnormalities as compared to the paper-electrophoretic method. The lipid dye and riboflavin concentration of the gels used give a background that makes it easy to detect chylomicra in the sample gel and allows for densitometric semiquantitation of the lipoprotein fractions. The method is reliable, precise, and accurate.

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