PURIFICATION AND PROPERTIES OF BRAIN N‐ACETYL‐β‐HEXOSAMINIDASE A

Publisher Website
Google Scholar
Abstract
—N‐Acetyl‐β‐hexosaminidase A was purified to homogeneity from human and monkey brains by the conventional procedures followed by concanavalin A–Sepharose affinity chromatography. The optimal activity was observed at pH 4·5 for both enzyme preparations with both the aglycones N‐acetylglucosamine and N‐acetylgalactosamine derivatives. The Km values for hexosaminidase A from monkey brain were 0·26 mm and 0·04 mm respectively for N‐acetylglucosamine and N‐acetylgalactosamine. Km values obtained for glucosamine and galactosamine derivatives for the human brain hexosaminidase A were of the same order. The glycoprotein nature of the enzymes was established by the affinity towards concanavalin A as well as by the presence of sialic acid, galactose, glucose, mannose and hexosamines in the enzyme molecule from monkey brain.