Linked Life Data

11001437

Source:http://linkedlifedata.com/resource/pubmed/id/11001437

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2001-2-2
pubmed:abstractText
The ferric forms of the three human embryonic hemoglobins exhibit pH titration's with pKa values in the range 8.25-8.6, which correlate with the reduced proteins affinity for oxygen. Azide ions bind to each ferric protein in a process consisting of two separate binding steps. The equilibrium constants for this process are in the 10-30 microM range and can be assigned to the individual chain within the proteins as reactivity appears independent of the nature of the partner chain. The kinetics of the azide binding reactions occur on the second time scale at mM ligand concentrations and also indicate the presence of two distinct processes that have been assigned to each of the two chains within the proteins. Non of these processes indicate any evidence of heme-heme interactions within the ferric form of the proteins. These findings are discussed in comparison with previously reported properties of adult ferric hemoglobin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-103
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The ferric form of the three human embryonic hemoglobins and their reactions with azide ions.
pubmed:affiliation
School of Biological Sciences, University of Auckland, New Zealand. t.brittain@auckland.ac.nz
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.