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Comparison of the Major Proteins of Shark Myelin with the Proteins of Higher Vertebrates
Author(s) -
Tai F. L.,
Smith Ross
Publication year - 1984
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.1471-4159.1984.tb02695.x
Subject(s) - proteolipid protein 1 , myelin , glycoprotein , myelin proteolipid protein , biochemistry , antiserum , polyacrylamide gel electrophoresis , chemistry , gel electrophoresis , peptide , amino acid , biology , microbiology and biotechnology , antibody , myelin basic protein , central nervous system , immunology , endocrinology , enzyme
On gel electrophoresis in dodecyl sulphate solutions shark CNS myelin showed four bands close in mobility to the proteolipid protein of bovine CNS myelin. They had apparent molecular weights of 21,000, 26,000, 27,000, and 31,500. Unlike bovine proteolipid protein, all of these shark proteins were shown to be glycosylated by staining gels with the periodate‐Schiff reagent. Amino acid analyses of the polypeptides eluted from polyacrylamide gels indicated a high content of apolar amino acids and a composition approximating that of the P o protein of bovine peripheral nervous system (PNS) myelin, rather than that of the CNS proteolipid protein. The shark poly‐peptide of apparent molecular weight 31,500 was obtained by elution from dodecyl sulphate gels and antibodies raised against it in rabbits. By probing of electroblots with this antiserum the four shark CNS bands were shown to share common determinants with each other, with a major shark PNS protein and with sheep and chicken major PNS glycoproteins (P o ). The binding of antibody was unaffected by deglycosylation of the shark CNS polypeptides with anhydrous hydrogen fluoride. Together, these results appeared to establish that shark CNS myelin contains four proteins that are closely related to a major shark PNS protein and to the P o protein of higher species.