CRUDE MYOSIN FRACTIONS AS MEAT BINDERS
作者： D. G. SIEGEL , G. R. SCHMIDT
DOI: 10.1111/J.1365-2621.1979.TB03463.X
关键词: Extraction (chemistry) 、 Actin 、 Sarcoplasm 、 Yield (chemistry) 、 Binding ability 、 Myosin 、 Biology 、 Mole 、 Phosphate 、 Biochemistry
摘要: A model system designed for the Instron Universal Testing Machine to record peak force required separate pieces of meat at a binding junction was used measure ability various muscle protein fractions bond pieces. The abilities crude myosin preparations were found be significantly greater than either homogenate free fat and sarcoplasmic proteins, total or nonprotein control consisting salt, phosphate water. Crude extracted from pre- post-rigor bovine over short long extraction times with three extracting solutions, Guba-Straub, Hasselbach-Schneider Weber-Edsall, measured ability, yield mole ratio actin by scanning SDS-PAGE gels. Results showed that superior Guba-Straub Weber-Edsall myosins in both yield. Comparisons ratios when same conditions present higher proportion resulted ability. However, different present, did not always give These results imply ionic interactions are inculpated phenomenon.
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