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The separation of whale myoglobins with two-dimensional electrophoresis

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Abstract

Five myoglobins (sperm whale, Sei whale, Hubbs' beaked whale, pilot whale, and Amazon River dolphin) were examined using two-dimensional electrophoresis. Previous reports indicated that none of these proteins could be separated by using denaturing (in the presence of 8–9 M urea) isoelectric focusing. This result is confirmed in the present study. However, all the proteins could be separated by using denaturing nonequilibriumpH-gradient electrophoresis in the first dimension. Additionally, all the myoglobins have characteristic mobilities in the second dimension (sodium dodecyl sulfate), but these mobilities do not correspond to the molecular weights of the proteins. We conclude that two-dimensional electrophoresis can be more sensitive to differences in primary protein structure than previous studies indicate and that the assessment seems to be incorrect that this technique can separate only proteins that have a unit charge difference.

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This work was performed at Argonne National Laboratory while the author was a Laboratory-Graduate Participant. The program was administered by the Argonne Division of Educational Programs with funding from the U.S. Department of Energy. This research was supported by the U.S. Department of Energy, Office of Health and Environmental Research, under Contract No. W-31-109-ENG-38.

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Spicer, G.S. The separation of whale myoglobins with two-dimensional electrophoresis. Biochem Genet 26, 645–655 (1988). https://doi.org/10.1007/PL00020503

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