| pubmed-article:8579359 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8579359 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8579359 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:8579359 | lifeskim:mentions | umls-concept:C0019046 | lld:lifeskim |
| pubmed-article:8579359 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8579359 | lifeskim:mentions | umls-concept:C0066918 | lld:lifeskim |
| pubmed-article:8579359 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8579359 | pubmed:dateCreated | 1996-3-8 | lld:pubmed |
| pubmed-article:8579359 | pubmed:abstractText | In previous studies mono-3,5-dibromosalicyl-fumarate was used to introduce an intramolecular crosslink (pseudo-crosslink) in the beta cleft between hemoglobin beta subunits. Sedimentation velocity analysis indicated that the product had a mean molecular weight indicating a tetramer with low dissociability. The product had a P50 higher than that of native hemoglobin and a plasma retention time in the rat of about 3 h, i.e., four times longer than untreated hemoglobin. However, the product contained a fraction which was rapidly eliminated in the urine and which had a short plasma half-time of about 20 min, indicating the presence of a dissociable fraction. We have attempted to further enhance the tetrameric stability of hemoglobin and prevent urine elimination by positioning a longer chain carboxylic acid than fumaric acid into the beta cleft. We reason that a longer molecule would allow for greater stabilizing interactions across the beta cleft. In the present study human and bovine hemoglobins were reacted with mono-3-5-dibromosalicyl muconate. Muconic acid is two carbons longer than fumaric acid. The products were acylated at the beta 82 (human) and beta 81 (bovine) lysines of the beta-cleft and had a low degree of dissociability. For reasons not presently understood, urine excretion was high and plasma half-time was not increased above that of untreated hemoglobin. In conclusion, it appears that only covalently crosslinked hemoglobins which are completely nondissociable tetramers escape filtration; tetramers with any degree of dissociability into dimers are filterable. | lld:pubmed |
| pubmed-article:8579359 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8579359 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8579359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8579359 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8579359 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8579359 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:8579359 | pubmed:author | pubmed-author:CollinsJ HJH | lld:pubmed |
| pubmed-article:8579359 | pubmed:author | pubmed-author:BucciEE | lld:pubmed |
| pubmed-article:8579359 | pubmed:author | pubmed-author:FronticelliCC | lld:pubmed |
| pubmed-article:8579359 | pubmed:author | pubmed-author:RazynskaAA | lld:pubmed |
| pubmed-article:8579359 | pubmed:author | pubmed-author:Matheson-Urba... | lld:pubmed |
| pubmed-article:8579359 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8579359 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8579359 | pubmed:volume | 326 | lld:pubmed |
| pubmed-article:8579359 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8579359 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8579359 | pubmed:pagination | 119-25 | lld:pubmed |
| pubmed-article:8579359 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:meshHeading | pubmed-meshheading:8579359-... | lld:pubmed |
| pubmed-article:8579359 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8579359 | pubmed:articleTitle | Stabilization of the tetrameric structure of human and bovine hemoglobins by pseudocrosslinking with muconic acid. | lld:pubmed |
| pubmed-article:8579359 | pubmed:affiliation | Department of Biochemistry, School of Medicine, University of Maryland at Baltimore 21201, USA. | lld:pubmed |
| pubmed-article:8579359 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8579359 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8579359 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8579359 | lld:pubmed |
