VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Electrophoretic behavior of b1 integrin subunit from human smooth muscle

   
Belkin V.M., Kozlova N.I., Bychkova V.V., Chekhonin B.V.
PubMed Id: 9281220
Year: 1997  Volume: 43  Issue: 1  Pages: 13-19
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.
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Belkin V.M., Kozlova N.I., Bychkova V.V., Chekhonin B.V. (1997) Voprosy meditsinskoi khimii, 43(1), 13-19.
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