pubmed-article:3937555 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3937555 | lifeskim:mentions | umls-concept:C0035499 | lld:lifeskim |
pubmed-article:3937555 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
pubmed-article:3937555 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
pubmed-article:3937555 | pubmed:issue | 27 | lld:pubmed |
pubmed-article:3937555 | pubmed:dateCreated | 1986-4-7 | lld:pubmed |
pubmed-article:3937555 | pubmed:abstractText | Purified bovine rhodopsin was reductively methylated with formaldehyde and pyridine/borane with the incorporation of approximately 20 methyl groups in the protein. Rhodopsin contains 10 non-active-site lysines, which account for the uptake of the 20 methyl groups. The permethylated rhodopsin thus formed is active toward bleaching, regeneration with 11-cis-retinal, and the activation of the GTPase (G protein) when photolyzed. The critical active-site lysine of permethylated rhodopsin can be liberated by photolysis. This lysine can be reductively methylated at 4 degrees C. Methylation under these conditions leads to the incorporations of approximately 1.5 methyl groups per opsin molecule using radioactive formaldehyde, with the ratio of epsilon-dimethyllysine:epsilon-monomethyllysine:lysine being approximately 5:4:1. The modified opsin(s) can regenerate with 11-cis-retinal to produce a mixture of active-site methylated and unmethylated rhodopsins having a lambda max = 512 nm. Using [14C]formaldehyde and [3H]retinal followed by reduction of the Schiff base, digestion, and chromatography showed that the active-site N-methyllysine was bound to the retinal. Treatment of the methylated opsin mixture (containing 1.5 active-site methyl groups) with o-phthalaldehyde/mercaptoethanol to functionalize the opsin bearing unreacted lysine, followed by regeneration with 11-cis-retinal and chromatographic separation, led to the preparation of the pure active-site epsilon-lysine monomethylated rhodopsin with a lambda max = 520 nm, significantly shifted bathochromically from rhodopsin or permethylated rhodopsin.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:3937555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:language | eng | lld:pubmed |
pubmed-article:3937555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3937555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3937555 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3937555 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3937555 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:3937555 | pubmed:author | pubmed-author:RandoR RRR | lld:pubmed |
pubmed-article:3937555 | pubmed:author | pubmed-author:LongstaffCC | lld:pubmed |
pubmed-article:3937555 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3937555 | pubmed:day | 31 | lld:pubmed |
pubmed-article:3937555 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:3937555 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3937555 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3937555 | pubmed:pagination | 8137-45 | lld:pubmed |
pubmed-article:3937555 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:3937555 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:3937555 | pubmed:articleTitle | Methylation of the active-site lysine of rhodopsin. | lld:pubmed |
pubmed-article:3937555 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3937555 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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