Distribution of calcium activated neutral proteinase (mM CANP) in myelin and cytosolic fractions in bovine brain white matter.
The activity of calcium-activated neutral proteinase (mM CANP) was determined in homogenate, myelin and supernatant of bovine brain corpus callosum. The enzyme activity in homogenate and myelin was increased eleven and thirteen-fold respectively by Triton X-100. Myelin prepared by the method of Norton and Poduslo as well as by a modified method, was shown to contain most (more than 50%) of homogenate mM CANP activity. The specific activity was highest in myelin, and increased almost three times more than the homogenate. Supernatant only contained 17% of enzyme activity. It is concluded from these studies that mM CANP is tightly bound to the membrane and predominantly associated with the myelin sheath.
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000502:physiology*; D002154:Calpain / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002417:Cattle; D003337:Corpus Callosum / Q000201:enzymology* / Q000648:ultrastructure; D003600:Cytosol / Q000201:enzymology; D009186:Myelin Sheath / Q000201:enzymology / Q000648:ultrastructure; D011092:Polyethylene Glycols / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology
D011092:Polyethylene Glycols; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D002154:Calpain; D002118:Calcium