Purification of a novel serpin-like protein from bovine brain
| Autor: | Masahiro Kawabata, Kiyomi Saeki, Takashi Chikai, Jun Ohta, Masahiro Nishibori, Toshihiko Ubuka |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
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 |
| Zdroj: | Neuroscience Research. 24:47-52 |
| ISSN: | 0168-0102 |
| DOI: | 10.1016/0168-0102(95)00973-6 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect