Isolation and characterization of the 36-kDa d-mannose 6-phosphate receptor from porcine testis
✍ Scribed by Tadashi Baba; Ken Watanabe; Yuji Arai
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 634 KB
- Volume
- 177
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
A o-mannose 6-phosphate receptor was isolated from total membranes of porcine testis, and its interaction with ligands was examined. The receptor was a glycoprotein comprised of several 36-kDa sub-units with an isoelectric point (PI) of 6.1. The binding of the receptor to the insoluble phosphomannan core occurred in the absence of divalent cations, but was selectively stimulated by MnCl, and effectively inhibited by o-mannose 6-phosphate, D-fructose l-phosphate, and pentaman-nosy1 monophosphate. The phosphate group and HO-Z of o-mannose 6-phosphate are important in the receptor-ligand interaction, HO-4 probably contributes to a lesser extent, and HO-l seems to have no interaction.