QUANTITATIVE DETERMINATION OF LOW-SALT SOLUBLE PROTEIN PATTERNS OF BOVINE MUSCLES COOKED AT DIFFERENT TEMPERATURES, BY SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS

1980 ◽  
Vol 45 (4) ◽  
pp. 901-904 ◽  
Author(s):  
HUGO A. CALDIRONI ◽  
NICOLÁS G. BAZÁN
1989 ◽  
Vol 40 (3) ◽  
pp. 675 ◽  
Author(s):  
DJ Tucker ◽  
AHF Hudson ◽  
A Laudani ◽  
RC Marshall ◽  
DE Rivett

The proteins from a range of cashmere, mohair, angoratcashmere crossbred and wool fibre samples were extracted at pH 8 with 8 M urea containing dithiothreitol, and were then radiolabelled by S-carboxymethylation using iodo(2-14C) acetate. The proteins from each sample were examined by two dimensional polyacrylamide gel electrophoresis in which the separation in the first dimension was according to charge at pH 8.9 and in the second dimension according to apparent molecular weight in the presence of sodium dodecyl sulfate. After electrophoresis the proteins were detected by fluorography. Protein differences in keratin samples from some individual goats existed, although the overall protein patterns were similar. None of the differences were consistent with any one goat fibre type. The protein patterns obtained for fibre samples from individual cashmere goats showed some differences when compared to those found for commercial blends from the same country of origin, indicating that blending can mask any animal-to-animal variation. While the electrophoretic technique does not unequivocally distinguish between cashmere, mohair and angora/cashmere crossbred fibres it does differentiate between wool and goat fibres.


1983 ◽  
Vol 61 (11) ◽  
pp. 2919-2923 ◽  
Author(s):  
David R. Benson ◽  
Deborah Hanna

Procedures for estimating the diversity of Frankia isolates are described. Forty-three alder isolates were separated into six groups by comparing protein patterns obtained during sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) of whole-cell lysates. Thirty-five of the strains comprised group A and were indistinguishable from one another. Four strains were quite similar to a Comptonia peregrina isolate (CpI1) and were included in group C. Group D had two members and groups B, E, and F each had one member. The groupings were confirmed by hyphal morphology, colony appearance, and carbon source utilization patterns.


1996 ◽  
Vol 79 (6) ◽  
pp. 1466-1470 ◽  
Author(s):  
Emiko Mochizuki ◽  
Takao Yamamoto ◽  
Sumiko Suzuki ◽  
Hiroyuki Nakazawa

Abstract We developed a rapid and simple method for identifying garlic and garlic products using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) with silver staining. Samples were homogenized with 1 % SDS or 6M urea and centrifuged. Supernatant containing garlic proteins was mixed with the same volume of loading buffer containing SDS and mercaptoethanol, heated in boiling water for 2 min, and applied to the wells of a ready-to-use polyacrylamide gradient gel (4–20%). Electrophoresis was performed 20 mA constant current for 2 h. The gel was stained with a silver staining kit and dried. Protein patterns of garlic and garlic products are different from those of other Allium plants such as onion, rakkyo, and caucas. The method was used to analyze samples of spice and garlic clove products. Absence of protein bands in garlic extract products suggests the products may contain less proteins and/or denatured proteins.


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