1981
DOI: 10.1080/00021369.1981.10864621
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Myosin ATPase and Acto-Heavy Meromyosin ATPase in Normal and in Pale, Soft and Exudative (PSE) Porcine Muscle

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Cited by 2 publications
(1 citation statement)
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“…They further reported that the myofibrillar ATPase in PSE muscle had a reduced Vmax (maximum velocity of turnover of substrate in enzyme), but that Kapp [dissociation constant of acto-HMM, (heavy meromyosin), which measures the affinity of binding] was unchanged. They concluded that the basic malfunctions in PSE muscle were the irreversible binding of myosin to the actin filaments and functional damage to the myosin ATPase (Sung et al 1981). Myosin extraction occurs via depolymerisation of the thick filament backbone (promoted by rising ionic strength and presence of pyrophosphate) and dissociation of the myosin heads from actin (promoted by NaCl and pyrophosphate in the presence of Mg 2+ ) (Parsons and Knight 1990).…”
Section: Myofibrillar Proteins and Myosin Atpase Activitymentioning
confidence: 99%
“…They further reported that the myofibrillar ATPase in PSE muscle had a reduced Vmax (maximum velocity of turnover of substrate in enzyme), but that Kapp [dissociation constant of acto-HMM, (heavy meromyosin), which measures the affinity of binding] was unchanged. They concluded that the basic malfunctions in PSE muscle were the irreversible binding of myosin to the actin filaments and functional damage to the myosin ATPase (Sung et al 1981). Myosin extraction occurs via depolymerisation of the thick filament backbone (promoted by rising ionic strength and presence of pyrophosphate) and dissociation of the myosin heads from actin (promoted by NaCl and pyrophosphate in the presence of Mg 2+ ) (Parsons and Knight 1990).…”
Section: Myofibrillar Proteins and Myosin Atpase Activitymentioning
confidence: 99%