ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
A model system designed for the Instron Universal Testing Machine to record the peak force required to separate pieces of meat at a binding junction was used to measure the ability of various muscle protein fractions to bond meat pieces. The binding abilities of crude myosin preparations were found to be significantly greater than the binding ability of either a muscle homogenate free of fat and sarcoplasmic proteins, a total muscle homogenate or a nonprotein control consisting of salt, phosphate and water. Crude myosin fractions extracted from pre- and post-rigor bovine muscle over short and long extraction times with three extracting solutions, Guba-Straub, Hasselbach-Schneider and Weber-Edsall, were measured for binding ability, yield and mole ratio of myosin to actin by scanning SDS-PAGE gels. Results showed that the Hasselbach-Schneider myosin was superior to the Guba-Straub and Weber-Edsall myosins in both binding ability and yield. Comparisons of mole ratios with binding abilities showed that when the same extracting conditions were present the higher proportion of myosin resulted in a higher binding ability. However, when different extracting conditions were present, the higher proportion of myosin did not always give a higher binding ability. These results imply that ionic interactions are inculpated in the binding phenomenon.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1979.tb03463.x
