Linked Life Data

2751669

Source:http://linkedlifedata.com/resource/pubmed/id/2751669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-14
pubmed:abstractText
The binding of carbonmonoxyheme to semi-alpha-hemoglobin and to an apohemoglobin control was investigated using stopped-flow techniques in 0.025 M potassium phosphate buffer, pH 7 and 10 degrees C. The resultant second order kinetic data were analyzed by the classical model which assumes the existence of an intermediate complex which either redissociates to reactants or undergoes an irreversible conversion to form hemoglobin. The rate constants for the latter unimolecular process were apparently not experimentally different for semi-alpha-hemoglobin and apohemoglobin (360 ( +/- 100) s-1 and 480 ( +/- 60) s-1, respectively). However, the equilibrium dissociation constant for the intermediate of semi-alpha-hemoglobin (Kd = 9.3 ( +/- 2.6) micromolar) was approximately two fold greater than that of apohemoglobin (Kd = 4.1 ( +/- 0.5) micromolar). The reduced stability of the semi-alpha-hemoglobin complex was postulated to be due to the lower affinity of the beta pocket for heme. The studies reported here address the possible role of semi-alpha-hemoglobin as an intermediate in the assembly of hemoglobin in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
522-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Kinetics of heme binding to semi-alpha-hemoglobin.
pubmed:affiliation
Chemistry Department, University of Lowell, MA 01854.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.