Primary structure of equine myelin basic protein by mass spectrometry.
Equine myelin basic protein (MBP) has been isolated from spinal cord and shown to consist of a number of components (charge isomers) by alkaline-urea gel electrophoresis. Mass analyses of several of these components showed that each was posttranslationally modified and some have been identified. Component 1, the most cationic charge isomer, was sequenced by a combination of liquid chromatography and mass spectrometry of peptides obtained by proteolytic digestion. At 172 residues it is slightly larger than the bovine (169) and the human (170). A major difference between bovine and equine sequences was the replacement of AQGH (bovine residues 76-79) by SRDG (equine). A number of other replacements involving single amino acids were also found. Methylated arginine (residue 108 equine) was found as both the mono- and the dimethylated derivative and represents the first MS/MS evidence for this modification in any MBP.
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Structural Biology and Biochemistry, The Hospital for Sick Children, Ont., M5G 1X8, Toronto, Canada.
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Freer
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Harauz
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Moscarello
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D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002412:Cations; D002417:Cattle; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006736:Horses; D006801:Humans; D008297:Male; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D002412:Cations; D004676:Myelin Basic Protein