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.
Sim
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Department of Medicine and Clinical Science, John Curtin School of Medical Research, Australian National University, Canberra.
White
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Denborough
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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