Linked Life Data

2494177

Source:http://linkedlifedata.com/resource/pubmed/id/2494177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1989-4-25
pubmed:abstractText
Hypoxic or anemic goats with the A hemoglobin genotype switch to the production of hemoglobin C, resulting in a reduced blood oxygen affinity. However, the physiologic consequences of this switch are not clear. We therefore studied the gas exchange properties of the two hemoglobin types. We found that purified hemoglobins A and C have very similar oxygen affinities and H+ Bohr effects, but in the presence of CO2, the affinity of hemoglobin C is substantially less than that of hemoglobin A. That this is not a nonspecific ionic effect is suggested by identical effects of NaCl on O2 binding to the two proteins and by a 2-fold higher capacity of hemoglobin C to bind CO2. The data can be explained by a class of CO2 binding sites in the beta C chain whose affinity is much higher than that of either of the primary sites or of those in Hb A. Our results suggest that in hemoglobin C-containing red cells CO2 acts as a potent allosteric effector, analogous to the role played by 2,3-diphosphoglycerate in human red blood cells. Goat hemoglobin C may have advantages over hemoglobins A or B in O2 transport under hypoxic conditions or in anemia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4812-7
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Gas exchange properties of goat hemoglobins A and C.
pubmed:affiliation
Division of Blood Research, Letterman Army Institute of Research, San Francisco, California 94129.
pubmed:publicationType
Journal Article