Thiophosphorylation of skeletal muscle sarcoplasmic reticulum in porcine malignant hyperpyrexia.
1. The basal, Ca2+-dependent and Mg2+-dependent thiophosphorylation of malignant hyperpyrexia-susceptible (MHS) porcine skeletal muscle was investigated. 2. Seven major proteins of Mr 100,000-11,000 were substrates for thiophosphorylation. 3. Sodium molybdate significantly elevated all levels of thiophosphorylation in control sarcoplasmic reticulum, but did not effect the Ca2+-dependent thiophosphorylation of MHS samples. 4. These results suggest that MHS sarcoplasmic reticulum may have altered sensitivity to protein phosphatase inhibition.
Department of Medicine and Clinical Science, John Curtin School of Medical Research, Australian National University, Canberra.
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White
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Denborough
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D008305:Malignant Hyperthermia / Q000378:metabolism / Q000662:veterinary*; D009132:Muscles / Q000378:metabolism*; D010750:Phosphoproteins / Q000302:isolation & purification; D011506:Proteins / Q000378:metabolism; D012016:Reference Values; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013552:Swine; D013553:Swine Diseases / Q000378:metabolism*
D010750:Phosphoproteins; D011506:Proteins; D013438:Sulfhydryl Compounds; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate; D008274:Magnesium; D002118:Calcium