The glycosylation of human myelin basic protein at threonines 95 and 98 occurs sequentially.
Human myelin basic protein (MBP) was glycosylated by the enzyme, UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase (EC 2.4.2.41). A maximum of 1.7 mol of GalNAc was transferred to basic protein on threonines 95 and 98 of the protein. Proton NMR studies of basic protein glycosylated with 0.48-1.7 mol of GalNAc/mol of MBP showed that the order of addition to the two threonine residues is not random but sequential. The Thr-95 resonances shifted downfield, followed by the downfield shift of the Thr-98 resonances with increasing glycosylation. Since this peptide segment of the molecule is highly structured, conformational factors are probably responsible for this directed addition.
Persaud
R
R
Research Institute, Hospital for Sick Children, Toronto, Canada.
Fraser
P
P
Wood
D D
DD
Moscarello
M A
MA
D000595:Amino Acid Sequence; D006031:Glycosylation; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000378:metabolism*; D011487:Protein Conformation; D013912:Threonine / Q000378:metabolism*
D004676:Myelin Basic Protein; D013912:Threonine