PMID: 9178554May 1, 1997Paper

Thermal gelation profile changes in reconstituted actomyosin due to storage under a high salt concentration and low temperature

Bioscience, Biotechnology, and Biochemistry
H TanjiA Suzuki

Abstract

Changes in the heat-induced gelation properties of reconstituted rabbit skeletal actomyosin stored under a high salt concentration at pH 6.0 and 0 degree C were investigated at different weight ratios of actin to myosin by using dynamic rheological and biochemical measurements. The addition of actin resulted in a pronounced peak maximum at about 50 degrees C and an accompanying temporary reduction in the range at about 50 degrees C to 60 degrees C. The more the initial actin concentration was increased, the greater was the area of the peak/shoulder. However, this area was markedly diminished with increasing storage time. As a result, the dynamic rheological pattern was transformed from an actomyosin type into a myosin type. The relationship between the G' value at 80 degrees C and the actin/myosin weight ratio was curvilinear, with a peak at the ratio of 0.05, immediately after storage was started. This profile changed during storage, depending on the extent to denaturation of actin and myosin in the reconstituted actomyosin (RAM). The G' value of actomyosin in 0.5 M KCl with a small actin/myosin ratio of 0.05 decreased to one-half of its initial value after 7 days of storage, whereas the G' value with a large actin/myosin rati...Continue Reading

References

Jan 1, 1982·Methods in Cell Biology·J D Pardee, J A Spudich

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Citations

Jul 3, 2009·Journal of the Royal Society, Interface·Maria Grazia OrtoreDaniela Russo

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