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Role of light chains in heat-induced gelation of skeletal muscle myosin
Ist Teil von
Journal of food science, 1991-05, Vol.56 (3), p.855-856
Ort / Verlag
Oxford, UK: Blackwell Publishing Ltd
Erscheinungsjahr
1991
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
More than 60% of alkali light chains were released from rabbit skeletal myosin during heating to form get. The removal of about 1 mol of regulatory light chain (LC2)/mol of myosin (LC2-deficient myosin) resulted in major decrease of gel strength at low ionic strength. The F-actin concentration required to attain maximum gel strength of the LC2-deficient myosin was greater than that of control myosin. These changes in functional characteristics of myosin induced by removal of LC2 were restored by reassociation of LC2 to the LC2-deficient myosin. Results showed skeletal myosin LC2 has an important role in its heat-induced gelation