Characterization of turkey myelin basic protein isolated by a simple procedure.
Highly purified basic proteins have been isolated from bovine and turkey brains by a novel method employing acid-acetone extraction. The final product gave a single band on polyacrylamide gel electrophoresis at pH 4.3 and in the presence of sodium dodecyl sulfate. Both proteins have arginine at the COOH-terminus while the NH2-terminal residue cannot be detected and is probably blocked. A higher ratio of histidine to lysine and a greater proportion of serine and valine was found for the turkey compared with the bovine protein. Both proteins contain one tryptophan and two methionine residues. However, it was found from cyanogen bromide treatment that there is a marked difference in the location of one of the methionine residues, while the tryptophan-containing peptides liberated after trypsin digestion have different mobilities on peptide maps. When dissolved in water these proteins give a typical random coil curve from circular dichroism (CD), whereas in 80% methyl alcohol they assume a 25% alpha-helix.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000378:metabolism; D002417:Cattle; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D003488:Cyanogen Bromide; D004590:Electrophoresis, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D008722:Methods; D004676:Myelin Basic Protein / Q000032:analysis* / Q000302:isolation & purification; D014422:Turkeys
D000596:Amino Acids; D004676:Myelin Basic Protein; D003488:Cyanogen Bromide