Endo-N-acetyl-β-D-glucosaminidase activity in rat liver. Studies on substrate specificity, enzyme inhibition, subcellular localization and partial purification
- 15 July 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 229 (2) , 379-385
- https://doi.org/10.1042/bj2290379
Abstract
Endo-N-acetyl-.beta.-D-glucosaminidase (EC 3.2.1.96, endoglucosaminidase) was partially purified (520-fold with resepct to the cytoplasmic activity) by using concanavalin A-Sepharose, CM-Sephadex and Bio-Gel P-150 chromatography. From the influence of exogenous glycopeptides on the endoglucosaminidase activity it can be concluded that this activity consists of 1 enzyme hydrolyzing both N-acetyl-lactosaminic-type and oligomannosidic-type substrates. Glycoproteins present in the homogenate inhibit the endoglucosaminidase activity. On reexaminaton of the subcellular distribution of endoglucosaminidase (after removal of inhibiting glycoproteins from the resepctive subcellular fractions), its cytoplasmic localization was confirmed.This publication has 22 references indexed in Scilit:
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