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ALTERATION OF MYELIN BIOSYNTHESIS IN SLICES OF RABBIT SPINAL CORD BY ANTISERUM TO MYELIN BASIC PROTEIN AND BY PUROMYCIN 1
Author(s) -
Pellkofer R.,
Jatzkewitz H.
Publication year - 1976
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.1471-4159.1976.tb12252.x
Subject(s) - puromycin , antiserum , myelin , spinal cord , tyrosine , myelin basic protein , biochemistry , chemistry , microbiology and biotechnology , biology , central nervous system , protein biosynthesis , antibody , endocrinology , immunology , neuroscience
— Slices of rabbit spinal cord were incubated with [ 3 H]tyrosine and [ 35 SO 4 ] in the presence of either 5% antiserum to myelin basic protein or 0.21 mM‐puromycin. The degree of incorporation of the precursors into the basic protein (BP), the proteolipid protein (PLP) and into sulphatides, as a representative lipid, in isolated myelin was investigated. Anti‐BP serum inhibited the incorporation of [ 3 H]tyrosine into BP and PLP from 22 to 46% as compared to controls, whereas puromycin nearly completely inhibited incorporation. The incorporation of [ 35 SO 4 ] into sulphatides was inhibited by anti‐BP serum from 20 to 34% and by puromycin from 33 to 65% as compared to controls. These alterations were myelin‐specific as shown by the equal or even increased incorporation of the precursors into the homogenates of spinal cord. The results are discussed in relation to the interaction of lipids and proteins in membrane assembly.