PRODUCTION AND CHARACTERIZATION OF THE MONOCLONAL-ANTIBODY AGAINST SGP120, A NOVEL SERUM-PROTEIN

A monoclonal antibody designated B1.9.E-2 was produced and characteriz ed to facilitate study of the immunizing antigen-a serum glycoprotein of 120 kDa (sgp 120) of unknown function. The antibody, produced in mi ce, reacts with 1-2 epitopes located in the N-terminal region of the s gp 120 molecule, The affinity of the reaction, as determined by Scatch ard analysis, is K-a = 1.13 x 10(10) l/M and is of a hydrophobic natur e, The monoclonal antibody can be purified to a high degree by a modif ied caprylic acid method and by protein G FPLC chromatography column. B1.9.E-2 does not trigger the complement cascade, as determined by C3 RIA and immune complex solubilization assays, Both affinity purified ( C4b Sepharose) and chromatographically isolated (using jacqualine agar ose) sgp 120 were recognized by B1.9.E-2. The monoclonal antibody can be utilized for affinity purification of sgp 120, for detection of int act or cleaved sgp 120 in biological samples of healthy and ill indivi duals, and for the number of functional and neutralization assays aime d at resolving the physiologic role of sgp 120.