A new epitope on human myelin basic protein arising from cleavage by a metalloendoprotease associated with brain myelin membranes.
Human brain myelin membranes were incubated to allow activity of an associated metalloendoprotease which cleaves myelin basic protein (MBP). A 10.3 kDa C-terminal fragment of MBP, peptide C, isolated from the incubation medium had a blocked N-terminal. After treatment with pyroglutamyl aminopeptidase, N-terminal sequencing indicated that Gln74 of MBP formed the N-terminal residue of peptide C. A rabbit antiserum was raised to a synthetic peptide containing the sequence Pyroglu-Lys-Ser-His-Gly-Arg, corresponding to the first six residues of peptide C. By immunoblotting this serum reacted with peptide C but not with intact MBP. The data indicate that cleavage of MBP by a myelin-associated protease engenders a new epitope.
Groome
N
N
Department of Neurochemistry, Institute of Neurology, London, U.K.
Chantry
A
A
Earl
C
C
Newcombe
J
J
Keen
J
J
Findlay
J
J
Glynn
P
P
D000595:Amino Acid Sequence; D000939:Epitopes; D006801:Humans; D007163:Immunosorbent Techniques; D008666:Metalloendopeptidases / Q000378:metabolism*; D004676:Myelin Basic Protein / Q000276:immunology*; D009186:Myelin Sheath / Q000201:enzymology*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000276:immunology; D010446:Peptide Fragments / Q000276:immunology
D000939:Epitopes; D004676:Myelin Basic Protein; D009842:Oligopeptides; D010446:Peptide Fragments; D008666:Metalloendopeptidases