Linked Life Data

2037047

Source:http://linkedlifedata.com/resource/pubmed/id/2037047

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-7-2
pubmed:abstractText
Equilibrium and kinetic experiments on site-directed mutants of a synthetic sperm whale myoglobin (Mb) gene have been performed. Results on the reactivity on both ferric and ferrous wild type and mutants Mb's are presented. Analysis of ligand binding to His (E7) Val and His (E7) Val-Thr (E10) Arg mutants compared to wild-type sperm whale, horse and Aplysia limacina Mb's, shows that the introduction of an arginyl residue at the topological position E10 greatly enhances the stability of the various Mg:heme ligand adducts. Alternative mechanisms of ligand stabilization may therefore be operative in Mb's lacking the distal histidine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Control and recognition of anionic ligands in myoglobin.
pubmed:affiliation
Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't