E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures: effects of quaternary structure.
Int J Biol Macromol
; 13(5): 289-94, 1991 Oct.
Article
em En
| MEDLINE
| ID: mdl-1666299
ABSTRACT
Photolysis of nitrosyl haemoglobin (HbNO) has been studied from 6.5 K to 20 K for different NO saturation conditions. The kinetic curves are fitted equally well by a biphasic exponential and a distribution of activation energies. The parameters are straightforwardly related to the quaternary structure of the protein. The biphasic model indicates that two germinate processes in the NO reassociation to Hb dominate at low temperatures independent of the protein conformation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemoglobinas
Tipo de estudo:
Health_economic_evaluation
Limite:
Humans
Idioma:
En
Ano de publicação:
1991
Tipo de documento:
Article