pubmed-article:8407928 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0034266 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0916181 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0060520 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C1148923 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C1548779 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C1947902 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C2827499 | lld:lifeskim |
pubmed-article:8407928 | lifeskim:mentions | umls-concept:C1167624 | lld:lifeskim |
pubmed-article:8407928 | pubmed:issue | 28 | lld:pubmed |
pubmed-article:8407928 | pubmed:dateCreated | 1993-11-24 | lld:pubmed |
pubmed-article:8407928 | pubmed:abstractText | Sarcoplasmic reticulum vesicles were treated with 2 mM pyridoxal 5'-phosphate (PLP) at 25 degrees C and pH 7.0 for 6 min and reduced by NaBH4. Both the activity of the Ca(2+)-ATPase and the capacity for high affinity Mg-ATP binding were greatly reduced. Acetyl phosphate hydrolysis or phosphoenzyme formation from Pi was not inhibited. The enzyme was protected by high affinity Mg-ATP binding against the PLP-induced inhibition. A similar protective effect was obtained by Mg-AMP as well as by Mg-ADP. Acetyl phosphate or Pi gave no protection. The PLP-treated vesicles were solubilized in SDS, and the Ca(2+)-ATPase was purified by size exclusion high performance liquid chromatography (HPLC). Mapping the fluorescently labeled peptides in the tryptic digest by reversed phase HPLC revealed a single fluorescent peak, which was protected by Mg-ATP against labeling. Sequencing showed that Lys-492 is the residue labeled with PLP. These results demonstrate that Lys-492 is located in or near the ATP binding site but not in the phosphorylation site or the Pi binding site. When Lys-515 was entirely prelabeled with fluorescein 5-isothiocyanate (FITC), the subsequent labeling of Lys-492 with PLP was not prevented. This finding demonstrates that Lys-492 is located outside the FITC-binding region. It has been widely accepted that FITC occupies the adenosine-binding region within the ATP binding site. In contrast to FITC, Mg-AMP strongly inhibited the labeling of Lys-492 with PLP. These findings lead to the conclusion that Lys-492 is located outside the adenosine-binding region, most probably in or near the region occupied by the alpha-phosphoryl group of Mg-ATP bound to the ATP binding site. | lld:pubmed |
pubmed-article:8407928 | pubmed:language | eng | lld:pubmed |
pubmed-article:8407928 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407928 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8407928 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8407928 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8407928 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8407928 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8407928 | pubmed:author | pubmed-author:YamagataKK | lld:pubmed |
pubmed-article:8407928 | pubmed:author | pubmed-author:KanazawaTT | lld:pubmed |
pubmed-article:8407928 | pubmed:author | pubmed-author:DaihoTT | lld:pubmed |
pubmed-article:8407928 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8407928 | pubmed:day | 5 | lld:pubmed |
pubmed-article:8407928 | pubmed:volume | 268 | lld:pubmed |
pubmed-article:8407928 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8407928 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8407928 | pubmed:pagination | 20930-6 | lld:pubmed |
pubmed-article:8407928 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:8407928 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8407928 | pubmed:articleTitle | Labeling of lysine 492 with pyridoxal 5'-phosphate in the sarcoplasmic reticulum Ca(2+)-ATPase. Lysine 492 residue is located outside the fluorescein 5-isothiocyanate-binding region in or near the ATP binding site. | lld:pubmed |
pubmed-article:8407928 | pubmed:affiliation | Department of Biochemistry, Asahikawa Medical College, Japan. | lld:pubmed |
pubmed-article:8407928 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8407928 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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