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Unusual Phylogenetic Conservation of the N ‐Terminal Amino Acid Sequence of the Central Nervous System‐Specific Membrane Glycoprotein F3‐87‐8 (CNSgp130)
Author(s) -
Flanagan Brian F.,
Teplow David B.,
Dreyer William J.,
Fabre John W.
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.tb13001.x
Subject(s) - glycoprotein , monoclonal antibody , biology , peptide sequence , amino acid , biochemistry , membrane glycoproteins , phylogenetic tree , homology (biology) , conserved sequence , antibody , microbiology and biotechnology , genetics , gene
CNSgp 130 is a CNS‐specific membrane glycoprotein abundantly expressed throughout the mature mammalian CNS. The molecule is recognised by the mouse monoclonal antibody F3‐87‐8, which reacts with a determinant of CNSgp 130 common to all mammals tested to date. Rat and human CNSgp 130 were purified by a combination of F3‐87‐8 monoclonal antibody affinity and gel permeation chromatography, and the N ‐terminal amino acid sequence was determined by gas‐phase sequencing techniques. The results show a remarkable conservation of the N terminus of the CNSgp 130 polypeptide between rats and humans, with complete identity of the first 20 amino acid residues. There was an unusually high and phylogenetically conserved number of cysteines in this region. The sequence showed no homology to other known sequences and should prove useful in precisely identifying the relationship of CNSgp 130 to other CNS membrane molecules.