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Limited proteolysis of bovine myelin basic protein by calcium-dependent proteinase from bovine spinal cord.

In order to shed some light on the role of proteinases in the process of demyelination in the central nervous system, a calcium-dependent proteinase was purified to homogeneity from bovine spinal cord, and its action on myelin basic protein purified from the same tissue was investigated. Among the three major myelin basic protein fractions, Fraction I was resistant to the action of the enzyme whereas Fractions II and III were degraded in the same manner, giving two major bands on SDS-polyacrylamide gel electrophoresis. The hydrolysis products were fractionated by high-performance liquid chromatography and characterized. The results showed that the myelin basic protein (Fractions II and III) was rather selectively cleaved at the Val93-Thr94 bond and the Arg96-Thr97 bond in mutually exclusive ways, with minor cleavages at the Ala16-Ser17 and Gly68-Ser69 bonds, suggesting the implication in vivo of calcium-dependent proteinase in the limited proteolysis of myelin basic protein.