| Literature DB >> 8573098 |
R Cacan1, C Dengremont, O Labiau, D Kmiécik, A M Mir, A Verbert.
Abstract
Neutral oligomannosides possessing one GlcNAc (OS-Gn1) and two GlcNAc (Os-Gn2) at the reducing end have been reported to be released during the N-glycosylation process in various biological models. To investigate which enzyme is responsible for OS-Gn1 formation, we used the Madin-Darby bovine kidney (MDBK) cell line which exhibits neither lysosomal chitobiase nor endoglucosaminidase activities. However, these cells produced OS-Gn1 and we showed that a neutral chitobiase is responsible for the transformation of OS-Gn2 into OS-Gn1. Using streptolysin O-permeabilized MDBK cells, we demonstrated that this neutral chitobiase activity is located in the cytosolic compartment and is active on oligomannoside species released during the N-glycosylation process.Entities:
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Year: 1996 PMID: 8573098 PMCID: PMC1216949 DOI: 10.1042/bj3130597
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857