| Autor: |
V M, Belkin, N I, Kozlova, V V, Bychkova, B V, Shekhonin |
| Rok vydání: |
1997 |
| Předmět: |
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| Zdroj: |
Voprosy meditsinskoi khimii. 43(1) |
| ISSN: |
0042-8809 |
| Popis: |
Total fraction of beta 1 integrin family was isolated from human smooth muscle by affinity chromatography on immobilized anti-beta 1 monoclonal antibodies. SDS-PAGE analysis and subsequent immunoblotting demonstrated that integrin samples contain unknown before high molecular mass (205 kD-nonreduced and 230 kD-reduced) material immunologically related to beta 1 integrin subunit. One dimensional peptide mapping showed that the 205 kD protein is not a novel beta 1 related integrin subunit, but a beta 1 integrin subunit dimer. Reduction of electrophoretic samples with dithiothreitol led to the removal of the major part of the beta 1 immunoreactive material from 205 kD to 130 kD region, indicating a disulfide nature of B1 integrin subunit dimer. The 230 kD protein turned out to be an only partly reduced beta 1 integrin disulfide bonded dimer. Possible in vivo existence of the disulfide bonded dimer and oligomer integrin forms is discussed. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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