Isolation and characterization of murine orthologue of PTP-BK

Takuya Tomemori, Naohiko Seki, Yo ichi Suzuki, Takahiko Shimizu, Hiroshi Nagata, Akiyoshi Konno, Takuji Shirasawa

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


We isolated and characterized a murine orthologue of PTP-BK, a receptor-type protein tyrosine phosphatase expressed in brain and kidney. The deduced amino acid sequences showed 89, 95, and 92% identities with human, rabbit, and chicken homologues of PTP-BK. Mouse PTP-BK encodes a polypeptide of 1,226 amino acids with calculated molecular weight of 138,598 Da. The mature form of PTP-BK constitutes of 3 domain structures including extracellular, transmembrane, and a single intracellular PTPase domain. Western blot analysis indicated that anti-PTP-BK antibody specifically immunoreacted to 2 distinct molecules of 200 kDa and 220 kDa in COS cells, possibly due to differential glycosylation. The recombinant PTP-BK showed the phosphatase activity specific for the phosphotyrosine, but not for the phosphoserine residue of phosphopeptides in vitro. Radiation hybrid panel assigned mouse PTP-BK gene to 5.02cR distal to from the marker D6Mit339 on chromosome 6. Mouse PTP-BK was classified in PTPRO family in novel nomenclature. We discuss here the diversity and physiological functions of PTPRO family of PTP. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)974-981
Number of pages8
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2000 Oct 5

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Isolation and characterization of murine orthologue of PTP-BK'. Together they form a unique fingerprint.

Cite this