Distribution of cholinesterases of rabbit skeletal muscle.
Two cholinesterase (ChE) fractions were extracted from homogenates of rabbit skeletal muscle. One of them the sarcoplasmic ChE could be dissolved quantitatively with solution A. Following the extraction with solution B the myofibrillar ChE fraction could be recovered. The ChE-activity of the sarcoplasmic extract was about 38% and the activity of myofibrillar extract was about 50% of the ChE-activity of muscle homogenates. According to our calculations about 10-12% of the total ChE-activity is insoluble. By the aid of PAGE seven zones of ChE-activity could be distinguished in the sarcoplasmic extract. The activity of myofibrillar ChE-fraction was obtained by chromatographic purification of LMM. The LMM1 proved to be inhomogeneous with PAGE, however, only one fraction displayed ChE-activity. Immune-serum produced against myosin did not give reaction with purified sarcoplasmic ChE, only with the myofibrillar fraction. Our results suggest that the heterogeneous distribution of muscle ChE-es in different molecular forms is not an artifact.
D000818:Animals; D002802:Cholinesterases / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits
D009124:Muscle Proteins; D002802:Cholinesterases