Characterization of Rauscher murine leukemia virus envelope glycoprotein receptor in membranes from murine fibroblasts.
AUTOR(ES)
Kalyanaraman, V S
RESUMO
Plasma membrane preparations from KA31 (mouse) cells contained receptors for the binding of Rauscher murine leukemia virus (R-MuLV) envelope glycoprotein, gp70. This binding was demonstrated by gel filtration of a mixture of the microsomal fraction of the cells and 125I-labeled gp70. A rapid and convenient assay was developed to measure the complex formation between the membrane receptors and gp70 involving specific precipitation of the complex by 3 to 4% polyethylene glycol. The complex formation was responsive to the concentrations of both the receptor and gp70 and also to changes in temperature and pH. The gp70 binding was a noncooperative, saturable process, and an association constant of 3.5 X 10(8) M-1 was estimated from the binding data. The complex formation was reversible and a near-total exchange of 125I-labeled gp70 in the complex was achieved by incubation with excess of unlabeled gp70. The complex formation was inhibited by protein denaturing agents, guanidine-hydrochloride and urea. Pretreatment of the membrane fractions with either chymotrypsin or phospholipase C led to a loss of the membrane-associated receptor activity, indicating that a lipoprotein structure was important for the receptor function, consistent with the observation that nonionic detergents strongly inhibited the complex formation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=525792Documentos Relacionados
- Binding characteristics of Rauscher leukemia virus envelope glycoprotein gp71 to murine lymphoid cells.
- Biochemical and Immunological Characterization of the Major Envelope Glycoprotein gp69/71 and Degradation Fragments from Rauscher Leukemia Virus
- Isolation of BPgp70, a fibroblast receptor for the envelope antigen of Rauscher murine leukemia virus.
- Structure of the murine leukemia virus envelope glycoprotein precursor.
- The role of envelope glycoprotein processing in murine leukemia virus infection.