The N-terminal domain I of human lactotransferrin binds specifically to phytohemagglutinin-stimulated peripheral blood human lymphocyte receptors.
FEBS Lett
; 255(1): 201-4, 1989 Sep 11.
Article
em En
| MEDLINE
| ID: mdl-2551729
ABSTRACT
Human lactotransferrin receptors have been recently characterized on mitogen-stimulated human lymphocytes [(1989) Eur. J. Biochem. 179, 481-487]. In order to define the lactotransferrin recognition site by these receptors, the binding to lymphocytes of several tryptic fragments, isolated from human lactotransferrin by mild tryptic hydrolysis [(1984) Biochim. Biophys. Acta 787, 90-96], has been investigated. The 30 kDa N-tryptic fragment (residues 4-281) and the re-associated N,C-tryptic complex bind to lactotansferrin lymphocyte receptor with a dissociation constant of 44 nM and 39 nM, respectively, similar to the value obtained for the native lactotransferrin (Kd = 46 nM). However, neither the N-terminal domain II (residues 91-257) nor the 50 kDa C-tryptic fragment (residues 282-703) are recognized. These results suggest that the binding site of human lactotransferrin by the lymphocyte receptor is located in the N-terminal lobe and more precisely in the N-terminal domain I (residues 4-90 and/or 258-281).
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Base de dados:
MEDLINE
Assunto principal:
Fito-Hemaglutininas
/
Linfócitos
/
Receptores de Superfície Celular
/
Lactoferrina
/
Lactoglobulinas
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1989
Tipo de documento:
Article
País de afiliação:
França