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Turbidity, Viscosity and ATPase Activity of Fibrillar Protein Extracts of Rabbit Muscle
Author(s) -
WEINER P. D.,
PEARSON A. M.,
SCHWEIGERT B. S.
Publication year - 1969
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1969.tb10349.x
Subject(s) - pyrophosphate , atp hydrolysis , chemistry , viscosity , hydrolysis , clearance , biochemistry , biophysics , atpase , magnesium , skeletal muscle , adenosine triphosphate , chromatography , enzyme , anatomy , biology , organic chemistry , thermodynamics , medicine , physics , urology
SUMMARY Results suggest that actomyosin from muscle in rigor is more easily dissociated than actomyosin from prerigor muscle. The addition of MgCl 2 decreased the rate of ATP hydrolysis and extended the clear phase of the fibrillar protein extract. Pyrophosphate in the presence of magnesium was as effective as ATP in clearing actomyosin. As the ATP was hydrolyzed, the viscosity of the solution returned to values greater than those obtained before the addition of ATP. However, samples cleared with pyrophosphate retained their low viscosity characteristics indefinitely.