Abstract
Abstract— Isolated bovine central nerve myelin sheath preparations showed non‐specific esterase activity towards naphthyl ester substrates of increasing chain length from acetate to palmitate. Short chain esters were hydrolysed much faster than long chain substrates by myelin, the specific activity for the hydrolysis of β‐naphthyl acetate being the highest. Micro‐somal fractions from brain white matter were much higher in esterase activity to all naphthyl ester substrates. NADPH‐cytochrome c reductase activity was absent from isolated myelin samples. Distilled water and salt and buffer solutions of different ionic strengths and pH were ineffective in releasing non‐specific esterase activity from myelin although tri‐potassium citrate caused marked inhibition of the membrane‐bound esterase activity. The detergent Triton X‐100 released esterase activity from the myelin preparations but at a concentration of 0.1 per cent was also inhibitory.
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