作者: Hidekazu Yamada , Motoyuki Shimonaka , Yu Yamaguchi , Kenya Shitara , Ken Watanabe
DOI: 10.1016/S0021-9258(17)32144-0
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摘要: Abstract By using polyclonal antiserum, which recognizes multiple proteoglycan core proteins, we isolated a cDNA species for an unknown chondroitin sulfate in bovine brain. Unexpectedly, DNA sequencing revealed that the encodes open reading frame highly homologous to human receptor-type protein-tyrosine phosphatase, RPTP beta. To prove beta is proteoglycan, raised three antibodies against extracellular and cytoplasmic domains of These have been shown react with smear band ranging from 350 500 kDa brain extracts. Digestion chondroitinase ABC eliminated this gave rise 310/300-kDa doublet was not detected without digestion, indicating almost all molecules contain chains. In cerebellum, immunofluorescence staining chondroitinase-treated sections pericellular localization external internal granular layers. data establish expressed constitutively as brain, suggest sulfates may be essential component physiological function vivo.