Further evidence of dimer-tetramer transition in hemoglobin from Liophis miliaris
Braz. j. med. biol. res
;
20(6): 861-4, 1987. ilus
Article
in English
| LILACS
| ID: lil-77467
RESUMO
Liophis miliaris hemoglobins in the stripped form exhibit a high oxigen affinity, a small alkaline Bohr effect, a pronounce organic polyphosphate effect and a pH-dependent Hill coefficient, close to 2 below pH 7.5 and near 1 at higher pHs. Molecular weight determinations indicate 2 forms, a dimeric form of MW 32000 d. and a tetrameric form of about 64000 d. The deoxyhemoglobin is tetrameric. Ion-exchange chromatography shows two components which may bind to each other being eluted as a single component of MW 32000 d. The osygen alkaline Bohr effect observed for the stripped hemoglobin may be explained by the transition from the tetramer to the dimer during oxygen addition experiments. The phenomenon appears to be unique among animals. ß-Chain sequencing determinations show that abnormal human hemoglobin with similar properties has a glutamic acid residue substituted at the alfa1-ß2 interface by valine in snake hemoglobin
Search on Google
Index:
LILACS (Americas)
Main subject:
Oxygen
/
Hemoglobins
Limits:
Animals
Country/Region as subject:
Asia
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
1987
Type:
Article
/
Congress and conference
Similar
MEDLINE
...
LILACS
LIS