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CHARACTERIZATION OF A RAT BRAIN FUCOSYL‐TRANSFERASE
Author(s) -
Broquet P.,
PerezGonzalez M. N.,
Louisot P.
Publication year - 1979
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.1471-4159.1979.tb00390.x
Subject(s) - transferase , isoelectric focusing , chemistry , fetuin , isoelectric point , characterization (materials science) , biochemistry , mechanism (biology) , substrate (aquarium) , enzyme , biophysics , biology , materials science , nanotechnology , physics , quantum mechanics , glycoprotein , ecology
— Rat brain fucosyl‐transferase was solubilized using Triton X–100 detergent, and then purified by electrofocusing. From studies of some exogenous glycoproteinic acceptors, desialylated fetuin appeared to be the most effective substrate. Study of initial velocity patterns gave evidence for a BiBi sequential mechanism, assumed to be a random BiBi with dead end inhibition.