Overview:

MBP exists as four major forms in the pig CNS with apparent molecular weights of 21.5K, 20.2K, 18.5K, and 17.3K (2). Native pig MBP is extracted under acidic conditions and further purified by cation chromatography. MBP is an efficient substrate for numerous protein kinases including ERK/MAP Kinase family, cAMP-dependent Protein Kinase, Calmodulin-dependent Protein Kinase, Protein Kinase C, and Phosphorylase Kinase (3, 4).

References:

1.Chevalier D, et al.Purification of myelin basic protein from bovine brain.Protein Expr Purif. 18(2):229-34, 2000.2.Sheng HZ, et al. Developmental study of myelin basic protein variants in various regions of pig nervous system. J Neurochem. 1989 Mar;52(3):736-40.3.Sanghera J. et al. Identification of the sites in myelin basic protein that are phosphorylated by meiosis-activated protein kinase p44mpk. FEBS Lett. 1990 Oct 29;273(1-2):223-6.4. Martenson, et al., Identification of multiple in vivo phosphorylation sites in rabbit myelin basic protein. J. Biol. Chem. 258: 930, 1983.