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DIFFERENTIAL INCORPORATION OF LYSINE INTO RETINAL PROTEIN FRACTIONS FOLLOWING FIRST EXPOSURE TO LIGHT
Author(s) -
Richardson K.,
Rose S. P. R.
Publication year - 1973
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.1471-4159.1973.tb05997.x
Subject(s) - lysine , labelling , acetylcholinesterase , retinal , biochemistry , glycoprotein , polyacrylamide gel electrophoresis , chemistry , retina , polyacrylamide , electrophoresis , chromatography , biology , enzyme , microbiology and biotechnology , amino acid , neuroscience
—Soluble and insoluble proteins from the retina of dark‐reared rats and from similar rats exposed to light for the first time, were subjected to electrophoresis on polyacrylamide gels. After injection of [ 3 H] or [ 14 C]lysine, using a double‐labelling technique, striking differences were observed in the pattern of incorporation into the forty‐one fractions investigated. After exposure for 1 h significant differences emerged in 13 of these fractions (High Differential Activity fractions) when compared with incorporation in control animals, a finding which persisted, irrespective of the order of labelling. Histochemical examination for acetylcholinesterase and glycoprotein material, showed the presence of these substances in some of the high differential activity fractions, and molecular weight determination was carried out on the insoluble fractions separated on SDS‐gels. It is concluded that the consistent enhancement of incorporation of precursor into retinal proteins which accompanies first exposure to light is a complex response involving a number of particular protein species, rather than a general elevation.