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Membrane‐bound N ‐acetyl‐β‐glucosamimdase
Author(s) -
Kato Goro,
Suzuki Yoshiyuki
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80156-3
Subject(s) - mannose , mannose 6 phosphate , biochemistry , intracellular , enzyme , fucose , receptor , chemistry , mannose 6 phosphate receptor , galactose , cell surface receptor , lysosome , growth factor
Several lysosomal enzymes solubilized at pH 4 from saponin‐treated membranes showed markedly variable affinities to the bovine liver phosphomannosyl receptor in both bovine and human livers. The enzymes from I‐cell disease liver did not bind the receptor in spite of normal intracellular activities. N ‐Acetyl‐β‐glucos‐aminidase was effectively released from the membrane preparation of a control liver by mannose 6‐phosphate, and other sugars showed little effect in this experiment. However, in the I‐cell disease liver, dissociation occurred not by mannose 6‐phosphate but by other sugars, such as fucose, mannose and N ‐acetyl‐D‐glucosamine. These results indicate the presence of an alternate transport system other than the pathway mediated by the mannose 6‐phosphate receptor, and the role of other sugar‐binding proteins is discussed in intracellular processing and transport of newly synthesized enzymes.