scholarly journals Methods for starch-gel electrophoresis of sarcoplasmic proteins. An investigation of the relative mobilities of the glycolytic enzymes from the muscles of a variety of species

1968 ◽  
Vol 107 (2) ◽  
pp. 139-150 ◽  
Author(s):  
R. K. Scopes
Keyword(s):  
Filter Paper ◽  
Enzyme Activities ◽  
Gel Electrophoresis ◽  
Detailed Comparison ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Muscle Proteins ◽  
Improved Method ◽  
Sarcoplasmic Proteins ◽  
Starch Gel

1. Details of an improved method for starch-gel electrophoresis of water-soluble muscle proteins are given. 2. Methods are described for detecting enzyme activities on the starch gel after electrophoresis, by using pieces of filter paper. 3. Compositions of incubation mixtures suitable for detecting any of the enzymes of glycolysis, and certain other enzymes, are given. 4. A comparison of the various enzymes in extracts of several muscles from one rabbit was made; most differences are quantitative only. 5. A detailed comparison of the mobilities of various enzymes in extracts of muscles from a wide variety of species was made. Each species was found to have a characteristic pattern of proteins on the starch gel, and the mobilities of individual enzymes varied considerably. 6. Potential uses and extensions of the methods are discussed.

Identification of Australian barley cultivars by laboratory methods: gel electrophoresis and gel isoelectric focusing of the endosperm proteins

1977 ◽  
Vol 17 (89) ◽  
pp. 1020 ◽  
Author(s):  
J McCausland ◽  
CW Wrigley
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Laboratory Methods ◽  
Barley Cultivars ◽  
Starch Gel ◽  
Electrophoretic Techniques ◽  
Gel Isoelectric Focusing

A range of laboratory methods was examined for their ability to distinguish between 19 barley cultivars currently grown in Australia. Aleurone colour, revealed after mechanical or chemical dehulling, differentiated Abyssinian, Atlas, Cape and Corvette from the other cultivars. Peroxidase and phenol testing were not useful. Seven different patterns were obtained for the hordeins of lowest mobility by starch gel electrophoresis. Further distinction was provided by flat gel isoelectric focusing of the water-soluble and hordein proteins for which 13 different pattern-groupings were obtained. The two electrophoretic techniques complemented one another, so that the use of both methods left only a few cultivars that could not be distinguished.

Improved Method for the Determination of Hemoglobin A2 by Starch-Gel Electrophoresis

1960 ◽  
Vol 6 (3) ◽  
pp. 254-262 ◽  
Author(s):  
C A J. Goldberg ◽  
A C Ross
Keyword(s):  
Sickle Cell ◽  
Gel Electrophoresis ◽  
Sickle Cell Trait ◽  
Starch Gel Electrophoresis ◽  
Improved Method ◽  
Starch Gel ◽  
Thalassemia Trait ◽  
Healthy Persons ◽  
Hemoglobin A2

Abstract It has been shown that variations in the preparation of the starch gel and in photographic interpretation can significantly affect the accuracy of the measurement of hemoglobin A2. An improved method for the determination of hemoglobin A2 by starch-gel electrophoresis has been presented which affords greater accuracy than was previously achieved. Hemoglobin A2 concentrations for healthy persons and patients with sickle cell trait, various nonthalassemic anemias, and thalassemia trait have been presented.

scholarly journals Bovine a-Lactalbumin C and aS1-, ß- and ?-Caseins of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

1981 ◽  
Vol 34 (2) ◽  
pp. 149 ◽  
Author(s):  
K Bell ◽  
KE Hopper ◽  
HA McKenzie
Keyword(s):  
Filter Paper ◽  
Gel Electrophoresis ◽  
Paper Electrophoresis ◽  
Northern Territory ◽  
Starch Gel Electrophoresis ◽  
Milk Samples ◽  
Starch Gel ◽  
The Common ◽  
Residue Substitution

An electrophoretic examination is made of milk samples taken from eight Bali (banteng) cattle, Bos (Bibos) javanicus, at Beatrice Hills, Northern Territory, Australia. Starch-gel electrophoresis at pH 8� 5 (NaOH-H3B03 buffer) and filter-paper electrophoresis at pH 8� 6 (diethylbarbiturate buffer) indicate that all samples contain a new a-lactalbumin variant, designated a-lactalbumin C. The order of mobility for bovine variants is A > B > C. The C variant differs from the common B variant in having one more amide residue (substitution of Asn for Asp or GIn for Glu).

INFLUENCE OF ALIEN GENOME COMBINATIONS ON PROTEIN SYNTHESIS IN CEREALS

1964 ◽  
Vol 42 (12) ◽  
pp. 1647-1657 ◽  
Author(s):  
F. C. Yong ◽  
A. M. Unrau
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Triticum Durum ◽  
Tetraploid Wheat ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Triticum Vulgare ◽  
Qualitative And Quantitative ◽  
Starch Gel ◽  
Variable Influence

Starch-gel electrophoresis of the water-soluble, salt-soluble, and alcohol soluble proteins of Triticale, Triticum durum, Secale cereale, Triticum vulgare, and Tritipyron revealed both qualitative and quantitative differences. The experimental evidence obtained indicated that the biosynthetic potential of the alien genomes in the synthetic species (Triticale) was not fully maintained. A variable influence of the tetraploid wheat (T. durum) genomes on protein synthesis in the three hexaploid cereals (Triticale, T. vulgare, and Tritipyron) was observed.

Muscle Proteins of the Coelacanth Latimeria Chalumnae Smith

1973 ◽  
Vol 53 (4) ◽  
pp. 763-784 ◽  
Author(s):  
G. Hamoir ◽  
A. Piront ◽  
Ch. Gerday ◽  
P. R. Dando
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
White Muscle ◽  
Protein Composition ◽  
Myofibrillar Proteins ◽  
Starch Gel Electrophoresis ◽  
High Concentration ◽  
Sarcoplasmic Proteins ◽  
Starch Gel ◽  
Muscle Types

Although the anatomy of the coelacanth muscles has been examined very thoroughly, their protein composition has, until recently, not been investigated. Thanks, however, to the 1972 British–French–American expedition to the Comores, frozen material has been made available and some results on myoglobin and four glycolytic enzymes have already been published. We have carried out a comparison of the sarcoplasmic proteins of red and white muscle by starch-gel electrophoresis. The ninhydrin-positive dialysable constituents and the myofibrillar proteins of white muscle have also been examined.A few puzzling results obtained with the white muscle extracts have been related to the occurrence of o.1 M ammonia, due presumably to the splitting of urea by a bacterial urease, and to an alteration of the active thiol groups of GAPDH and PK. If due account is taken of these unusual post-mortem changes, the extractability of the proteins and their properties are strikingly similar to those of teleosteans. The comparison of the sarcoplasmic proteins of white and red muscle by starch-gel electrophoresis revealed also that the differentiation observed in the coelacanth was similar to that occurring in the carp. A study of the low-molecular-weight proteins, or parvalbumins, of white muscle and of the myofibrillar proteins also shows the expected differences between the two muscle types.The only abnormal features observed in this study were the high concentration of parvalbumins, 1.5–2 times that found in other species examined, and the occurrence of an unusual globulin fraction which was easily extracted at ionic strength 0.5 and insoluble at ionic strength 0.35 and neutral pH.

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