2007
DOI: 10.1111/j.1748-1716.2007.01736.x
|View full text |Cite
|
Sign up to set email alerts
|

Lacking deoxygenation‐linked interaction between cytoplasmic domain of band 3 and HbF from fetal red blood cells

Abstract: The data indicate that HbF does not function as a transducer mediating O2 dependence of glycolysis in fetal red cells, in accordance with the different O2 and metabolic profiles compared to those in HbA-bearing adult red cells. In conjunction with the previously discovered O2 dependence of K+ transport in HbF-rich fetal cells, they moreover argue against linkage between different, physiologically relevant, O2-dependent red cell functions.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2011
2011
2024
2024

Publication Types

Select...
2

Relationship

0
2

Authors

Journals

citations
Cited by 2 publications
(1 citation statement)
references
References 33 publications
0
1
0
Order By: Relevance
“…Foetal hemoglobin (HbF) has a higher O 2 affinity than adult haemoglobin [ 64 ] and influences erythrocyte K + transport and O 2 dependence of erythrocyte glycolysis [ 65 ]. Increased HbO 2 affinity may result in enhanced lactate formation with subsequent decrease of HCO 3 - and thus increased CO 2 /HCO 3 - ratio.…”
Section: Discussionmentioning
confidence: 99%
“…Foetal hemoglobin (HbF) has a higher O 2 affinity than adult haemoglobin [ 64 ] and influences erythrocyte K + transport and O 2 dependence of erythrocyte glycolysis [ 65 ]. Increased HbO 2 affinity may result in enhanced lactate formation with subsequent decrease of HCO 3 - and thus increased CO 2 /HCO 3 - ratio.…”
Section: Discussionmentioning
confidence: 99%