Linked Life Data

6305406

Source:http://linkedlifedata.com/resource/pubmed/id/6305406

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1983-8-11
pubmed:abstractText
A fluorine NMR study of cyanomethemoglobin prepared from hemoglobin isolated from rabbits maintained on a diet containing DL-p-fluorophenylalanine is described. The results indicate that substitution of fluorophenylalanine occurs essentially randomly at all phenylalanine positions of the alpha- and beta-globin chains; a set of hybrid hemoglobins in which only the alpha- or only the beta-chains contain the fluorinated amino acid was prepared and used to ascertain the fluorine NMR signals arising from each chain. The temperature and pH dependences of chemical shifts, spin-lattice relaxation times, 19F(1H) nuclear Overhauser effects, and the effect of chemical modification of the beta-93 sulfhydryl groups were examined. When considered in light of presently available X-ray structures of human and horse hemoglobins, the available data permit a tentative assignment of most signals to particular fluorophenylalanine/phenylalanine positions in the globin sequences.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2076-87
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Assignment of fluorine nuclear magnetic resonance signals from rabbit cyanomethemoglobin.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.