Biochemical analysis of a 130,000 molecular weight glycoprotein on human melanoma cells.
Open Access
- 1 September 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 131 (3) , 1595-1599
- https://doi.org/10.4049/jimmunol.131.3.1595
Abstract
A monomeric sialoglycoprotein of 130,000 molecular weight (gp 130) is a membrane protein detected by mouse monoclonal antibodies on human melanoma cells and in lesser amounts on a wide range of normal and malignant cell types. Eight monoclonal antibodies reacting with gp 130 detect at least four spatially distinct epitopes on the exposed surface of the gp 130 molecule. Biosynthetic studies have shown that gp 130 is synthesized through two precursor forms: a 100 kD glycosylated species and an 80 kD unglycosylated species, presumably the primary translational product of the encoding mRNA.This publication has 2 references indexed in Scilit:
- Structural characterization of human melanoma-associated antigen p97 with monoclonal antibodies.The Journal of Immunology, 1981
- Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bondsArchives of Biochemistry and Biophysics, 1960