ArticleWillcox P, Hay C.
Comp Biochem Physiol B. 1978;61(1):1-12.
1. The beta-N-acetylglucosaminidase (EC 3.2.1.30) activities of human, pig, calf, lamb, rat and rabbit liver and plasma have been investigated. 2. All preparations had maximum activity between pH 4.0 and 4.5 and Km values with the substrate 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside ranged from 0.54 to 2.54 mM. 3. The isoenzyme profiles of liver and plasma beta-N-acetylglucosaminidase activity were compared using DEAE-cellulose chromatography. In all species the major anionic component of liver (beta-N-acetylglucsaminidase A) was eluted at a higher salt concentration than the most anionic plasma isoenzyme. 4. The plasma beta-N-acetylglucosaminidase A isoenzyme of all species contained sialic acid residues whereas only the rabbit, pig and calf liver isoenzymes were sialylated.