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Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self‐Association
Author(s) -
Milne Trudy J.,
Atkins Annette R.,
Warren Juanita A.,
Auton Wendy P.,
Smith Ross
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb04583.x
Subject(s) - association (psychology) , sequence (biology) , myelin basic protein , peptide sequence , myelin , biology , genetics , neuroscience , psychology , central nervous system , gene , psychotherapist
Myelin basic protein (MBP) from the Whaler shark ( Carcharhinus obscurus ) has been purified from acid extracts of a chloroform/methanol pellet from whole brains. The amino acid sequence of the majority of the protein has been determined and compared with the sequences of other MBPs. The shark protein has only 44% homology with the bovine protein, but, in common with other MBPs, it has basic residues distributed throughout the sequence and no extensive segments that are predicted to have an ordered secondary structure in solution. Shark MBP lacks the triproline sequence previously postulated to form a hairpin bend in the molecule. The region containing the putative consensus sequence for encephalitogenicity in the guinea pig contains several substitutions, thus accounting for the lack of activity of the shark protein. Studies of the secondary structure and self‐association have shown that shark MBP possesses solution properties similar to those of the bovine protein, despite the extensive differences in primary structure.