pubmed-article:9578561 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9578561 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:9578561 | lifeskim:mentions | umls-concept:C2347051 | lld:lifeskim |
pubmed-article:9578561 | lifeskim:mentions | umls-concept:C0065647 | lld:lifeskim |
pubmed-article:9578561 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:9578561 | pubmed:dateCreated | 1998-6-4 | lld:pubmed |
pubmed-article:9578561 | pubmed:abstractText | The stability of Mn(II) binding to manganese peroxidase (MnP) has been studied as a function of pH by spectrophotometric and potentiometric titrations. The sensitivity of the potentiometric titrations allows collection of data that are consistent with a high-affinity and a low-affinity Mn(II) binding site on the peroxidase. The two sites differ in affinity by 4 to 900-fold between pH 4 and 6.5. The stability of Mn(II) binding to the high-affinity site increases with increasing pH, while the stability of Mn(II) binding to the low-affinity site decreases with increasing pH. Interestingly, at pH values above 5.0, the high-affinity site appears to be partially unavailable for binding Mn(II). A pH-dependent structural change in the Mn(II) binding site is proposed to account for this partial inactivation at elevated pH. | lld:pubmed |
pubmed-article:9578561 | pubmed:language | eng | lld:pubmed |
pubmed-article:9578561 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9578561 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9578561 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9578561 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9578561 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9578561 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9578561 | pubmed:month | May | lld:pubmed |
pubmed-article:9578561 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:9578561 | pubmed:author | pubmed-author:GoldM HMH | lld:pubmed |
pubmed-article:9578561 | pubmed:author | pubmed-author:KishiKK | lld:pubmed |
pubmed-article:9578561 | pubmed:author | pubmed-author:MaukA GAG | lld:pubmed |
pubmed-article:9578561 | pubmed:author | pubmed-author:MaukM RMR | lld:pubmed |
pubmed-article:9578561 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9578561 | pubmed:day | 12 | lld:pubmed |
pubmed-article:9578561 | pubmed:volume | 37 | lld:pubmed |
pubmed-article:9578561 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9578561 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9578561 | pubmed:pagination | 6767-71 | lld:pubmed |
pubmed-article:9578561 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:9578561 | pubmed:meshHeading | pubmed-meshheading:9578561-... | lld:pubmed |
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pubmed-article:9578561 | pubmed:meshHeading | pubmed-meshheading:9578561-... | lld:pubmed |
pubmed-article:9578561 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9578561 | pubmed:articleTitle | pH-linked binding of Mn(II) to manganese peroxidase. | lld:pubmed |
pubmed-article:9578561 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada. | lld:pubmed |
pubmed-article:9578561 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9578561 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9578561 | lld:pubmed |