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- Publisher
- Wiley
- Copyright
- Copyright © 1986 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1742-464X
- eISSN
- 1742-4658
- DOI
- 10.1111/j.1432-1033.1986.tb09703.x
- Publisher site
- See Article on Publisher Site
Abstract
A processing mannosidase acting on (Man)9(GlcNAc)2 oligosaccharides, Man9 mannosidase, has been purified 2190‐fold from calf liver crude microsomes by a four‐step procedure involving (a) differential salt/detergent extraction, (b) affinity chromatography on AH‐Sepharose 4B with N‐5‐carboxypentyl‐1‐deoxy‐mannojirimycin as ligand, (c) ConA‐Sepharose and (d) DEAE‐Sephacel chromatography. (Man)9 mannosidase has a subunit molecular mass of 56 kDa and does not bind to ConA‐Sepharose, indicating the absence of high‐mannose oligosaccharides. The enzyme has a pH optimum close to pH 6.0 and requires divalent cations for activity, Ca2+ being most effective. It is inhibited by 1‐deoxymannojirimycin (dMM), N‐methyl‐dMM and N‐5‐carboxypentyl‐dMM with Ki= 7 μM, 75 μM, and 140 μM, respectively.
Journal
The Febs Journal – Wiley
Published: Jun 1, 1986