Purification of a novel serpin-like protein from bovine brain

Masahiro Nishibori, Takashi Chikai, Masahiro Kawabata, Jun Ohta, Toshihiko Ubuka, Kiyomi Saeki

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


We purified a novel serine proteinase inhibitor (serpin)-like protein from the bovine brain and named it B-43 from its molecular mass, 43 kDa. A cleaved peptide from B-43 was copurified with the native B-43. Partial amino acid sequencing of the purified B-43 showed that this protein was homologous to glia-derived nexin/protease nexin-1 (GDN/PN-1), plasminogen activator inhibitor 2, leukocyte elastase inhibitor (LEI) and placental thrombin inhibitor (PTI) among the serpins. Although B-43 had a similar amino acid composition to these serpins, the biochemical features of B-43 were different from them. B-43 did not form sodium dodecyl sulfate (SDS)-resistant serpin-proteinase complexes with thrombin, urokinase, pancreatic elastase and plasmin, suggesting that these proteinases were not the targets of B-43. In contrast to GDN/PN-1, B-43 did not have an affinity for heparin. B-43, having different biochemical properties from GDN/PN-1, appears to be an additional serpin expressed in the brain.

Original languageEnglish
Pages (from-to)47-52
Number of pages6
JournalNeuroscience Research
Issue number1
Publication statusPublished - Dec 1995


  • Bovine brain
  • Glia-derived nexin/protease nexin-1
  • Serine proteinase
  • Serine proteinase inhibitor

ASJC Scopus subject areas

  • Neuroscience(all)


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