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.
Belkin V.M., Kozlova N.I., Bychkova V.V., Chekhonin B.V. (1997) Electrophoretic behavior of b1 integrin subunit from human smooth muscle. Voprosy Meditsinskoi Khimii, 43(1), 13-19.
Belkin V.M. et al. Electrophoretic behavior of b1 integrin subunit from human smooth muscle // Voprosy Meditsinskoi Khimii. - 1997. - V. 43. -N 1. - P. 13-19.
Belkin V.M. et al., "Electrophoretic behavior of b1 integrin subunit from human smooth muscle." Voprosy Meditsinskoi Khimii 43.1 (1997): 13-19.
Belkin, V. M., Kozlova, N. I., Bychkova, V. V., Chekhonin, B. V. (1997). Electrophoretic behavior of b1 integrin subunit from human smooth muscle. Voprosy Meditsinskoi Khimii, 43(1), 13-19.
