Isolation and characterization of the 36-kDa D-mannose 6-phosphate receptor from porcine testis.
A D-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 MnCl2 and effectively inhibited by D-mannose 6-phosphate, D-fructose 1-phosphate, and pentamannosyl monophosphate. The phosphate group and HO-2 of D-mannose 6-phosphate are important in the receptor-ligand interaction, HO-4 probably contributes to a lesser extent, and HO-1 seems to have no interaction.
Baba
T
T
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Watanabe
K
K
Arai
Y
Y
D000818:Animals; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel; D006600:Hexosephosphates / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D008360:Mannosephosphates / Q000378:metabolism*; D008970:Molecular Weight; D017527:Receptor, IGF Type 2; D013552:Swine; D013737:Testis / Q000378:metabolism*
D002352:Carrier Proteins; D006600:Hexosephosphates; D008360:Mannosephosphates; D017527:Receptor, IGF Type 2