Comparison of adenylate kinase from normal and malignant hyperpyrexic porcine muscle.
Adenylate kinase has been implicated as a key factor in malignant hyperpyrexia, a complication of general anaesthesia which is usually triggered by the anaesthetic drug, halothane. Because of this, the enzyme was purified from both malignant hyperpyrexia susceptible and control porcine muscle. Electrophoretic studies, amino acid analysis, and peptide mapping of the purified enzymes revealed no significant differences between the two preparations. Both enzymes responded similarly to halothane and to the three sulfhydryl reacting reagents which were tested and they also showed an identical affinity for the substrate AMP. It is concluded that porcine MH is not due to an abnormality in the enzyme AK.
D000263:Adenylate Kinase / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006221:Halothane / Q000378:metabolism; D008305:Malignant Hyperthermia / Q000201:enzymology*; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D010770:Phosphotransferases / Q000032:analysis*; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013552:Swine
D000596:Amino Acids; D010446:Peptide Fragments; D013439:Sulfhydryl Reagents; D010770:Phosphotransferases; D000263:Adenylate Kinase; D006221:Halothane