1. Purification of a novel serpin-like protein from bovine brain
- Author
-
Masahiro Kawabata, Kiyomi Saeki, Takashi Chikai, Jun Ohta, Masahiro Nishibori, and Toshihiko Ubuka
- Subjects
Serine Proteinase Inhibitors ,Plasmin ,medicine.medical_treatment ,Molecular Sequence Data ,Receptors, Cell Surface ,Biology ,Serpin ,Serine ,Amyloid beta-Protein Precursor ,Thrombin ,medicine ,Animals ,Amino Acid Sequence ,Pancreatic elastase ,Serpins ,Brain Chemistry ,chemistry.chemical_classification ,Protease ,Superoxide Dismutase ,Immunochemistry ,General Neuroscience ,Brain ,General Medicine ,Molecular biology ,Amino acid ,Molecular Weight ,Protease Nexins ,carbohydrates (lipids) ,Biochemistry ,chemistry ,Plasminogen activator inhibitor-2 ,Cattle ,Carrier Proteins ,medicine.drug - Abstract
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.
- Published
- 1995