| pubmed-article:3166989 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0018976 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
| pubmed-article:3166989 | lifeskim:mentions | umls-concept:C1553628 | lld:lifeskim |
| pubmed-article:3166989 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:3166989 | pubmed:dateCreated | 1988-11-18 | lld:pubmed |
| pubmed-article:3166989 | pubmed:abstractText | Reported are the first examinations by 31P NMR of erythrocytes containing the non-heme iron O2-carrying protein hemerythrin (Hr). Intact coelomic erythrocytes from the sipunculids Phascolopsis gouldii and Themiste zostericola were shown by 31P NMR to contain O-phosphorylethanolamine and 2-aminoethylphosphonate as the major soluble phosphorus metabolites. This combination of major metabolites appears to be unique to sipunculan erythrocytes. Nucleoside triphosphates and mannose 1-phosphate were present in lower concentrations. The concentration of O-phosphorylethanolamine within P. gouldii erythrocytes was established to be greater than 20 mM. T. zostericola erythrocytes contained relatively high levels of 2-aminoethylphosphonate (on the order of 0.1 M) and lower levels of O-phosphorylethanolamine compared with those of P. gouldii. For P. gouldii and T. zostericola the intracellular pHs were determined to be 7.2 +/- 0.1 and 7.1 +/- 0.1, respectively, in air-equilibrated erythrocytes, and 6.5 +/- 0.1 in anaerobic P. gouldii erythrocytes. O-Phosphorylethanolamine was found to bind weakly to P. gouldii metHr (Kf approximately 7 M-1). This interaction is best characterized by either negative cooperativity or nonspecific binding. O-Phosphorylethanolamine strongly inhibits azide binding to the iron site of P. gouldii metHr at pH 7.2. The rate of azide binding decreases by approximately 85-fold in the presence of 0.33 M O-phosphorylethanolamine. However, neither O-phosphorylethanolamine nor 2-aminoethylphosphonate at 0.33 M was found to have any significant effect on O2 affinity of P. gouldii deoxyHr. Alternative functions for the two metabolites are suggested. | lld:pubmed |
| pubmed-article:3166989 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3166989 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3166989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3166989 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3166989 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3166989 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:3166989 | pubmed:author | pubmed-author:KurtzD MDMJr | lld:pubmed |
| pubmed-article:3166989 | pubmed:author | pubmed-author:RobitailleP... | lld:pubmed |
| pubmed-article:3166989 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3166989 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:3166989 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:3166989 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3166989 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3166989 | pubmed:pagination | 4458-65 | lld:pubmed |
| pubmed-article:3166989 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
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| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:meshHeading | pubmed-meshheading:3166989-... | lld:pubmed |
| pubmed-article:3166989 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3166989 | pubmed:articleTitle | 31P NMR probes of sipunculan erythrocytes containing the O2-carrying protein hemerythrin. | lld:pubmed |
| pubmed-article:3166989 | pubmed:affiliation | Department of Chemistry, Iowa State University, Ames 50011. | lld:pubmed |
| pubmed-article:3166989 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3166989 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
