Protein patterns of all samples were studied using SDS–PAGE described by Laemmli (1970). Solubilisation of gel samples with 5% sodium dodecyl sulfate solution (90 C) was carried out according to Morrissey, Wu, Lin, and An (1993). Stacking and separating gels were made using 4% (w/v) and 10% (w/v) acrylamide, respectively. Gels were fixed and stained with 0.125% Coomassie brilliant
blue R-250 (Bio-Rad, Richmond, CA, USA), and destained in a solution containing 50% methanol and 10% acetic acid. The molecular weight of the protein bands were determined by comparing the relative mobility of a protein standard (Kaleidoscope precision plus, Bio-Rad Laboratories, Hercules, CA, USA).
Protein patterns of all samples were studied using SDS–PAGE described by Laemmli (1970). Solubilisation of gel samples with 5% sodium dodecyl sulfate solution (90 C) was carried out according to Morrissey, Wu, Lin, and An (1993). Stacking and separating gels were made using 4% (w/v) and 10% (w/v) acrylamide, respectively. Gels were fixed and stained with 0.125% Coomassie brilliantblue R-250 (Bio-Rad, Richmond, CA, USA), and destained in a solution containing 50% methanol and 10% acetic acid. The molecular weight of the protein bands were determined by comparing the relative mobility of a protein standard (Kaleidoscope precision plus, Bio-Rad Laboratories, Hercules, CA, USA).
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