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Synaptosomal Sialyltransferase Glycosylates Surface Proteins that Are Inaccessible to the Action of Membrane‐Bound Sialidase
Author(s) -
Breen Kieran C.,
Regan Ciaran M.
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb00737.x
Subject(s) - sialyltransferase , sialidase , action (physics) , chemistry , biochemistry , enzyme , neuraminidase , physics , quantum mechanics
Sialyltransferase has been characterized in P2 pellets derived from animals of increasing age. The enzyme was found to be associated with the plasma membrane and to be developmentally regulated at times coincident with cell migration and fibre outgrowth. This regulation appeared to be due, in part, to an endogenous competitive inhibitor in the P2 pellet but not in the synaptosome. Optimal transfer of [ 14 C] N ‐acetylneuraminic acid to endogenous synaptosomal acceptors was achieved only in the absence of detergent. Furthermore, the transferred sialic acid was found to be inaccessible to the action of membrane‐bound sialidase. The significance of these findings is discussed.