Identification and purification of a chicken brain neuroglia-associated protein.
The identification, purification, and biochemical characterization of specific markers for neuroglial cells in the central nervous system is an essential step toward a better understanding of the function of glial cells. This manuscript reports the identification and purification of a neuroglia-associated protein (NAP-185) with an apparent molecular mass of 185 kDa. While its expression is not restricted to the brain, it was first identified in a specific subpopulation of glial cells when chick brain stem sections were analyzed with an affinity-purified rabbit antiserum raised against the catalytic domain of the T-cell protein tyrosine phosphatase. This 185-kDa antigen was purified to apparent homogeneity and confirmed to be responsible for the neuroglial staining observed. In spite of its immunological relation to T-cell protein tyrosine phosphatase, purified NAP-185 failed to display tyrosine phosphatase activity. The primary sequence of five NAP-185-derived peptides shows that this protein has not yet been characterized and that it is possibly related to AP180, a clathrin-associated protein.
Department of Biochemistry, University of Washington, Seattle 98195.
F F
FF
Solca
D I
DI
Lurie
C D
CD
Diltz
R S
RS
Johnson
S
S
Kumar
E W
EW
Rubel
E H
EH
Fischer
D000595:Amino Acid Sequence; D000818:Animals; D001253:Astrocytes / Q000737:chemistry*; D015415:Biomarkers; D001933:Brain Stem / Q000737:chemistry*; D002645:Chickens; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D014018:Tissue Distribution
D015415:Biomarkers; D009419:Nerve Tissue Proteins; C090154:neuroglia-associated protein 185 kDa