Effect of immunoglobulin G on membrane-bound enzyme activity of sarcoma 180 cells.
Changes in the activity of membrane bound ATPase of Sarcoma 180 cells caused by immunoglobulin G (IgG) of anti-Sarcoma 180 was investigated in relation to the incorporation of amino acid by the cells. Enzymatic activity of ATPase was increased up to 160% of the original activity upon incubation of the cell with IgG. Kinetic studies showed that IgG did not change the affinity of this enzyme for the substrate, but exerted influence upon catalytic efficiency of the enzyme. The rate of incorporation of leucine into Sarcoma 180 cells was also affected by IgG, as observed in the effect of IgG on the enzymatic reaction of the cells.
D000818:Animals; D000912:Antibodies, Neoplasm; D002448:Cell Adhesion; D002462:Cell Membrane / Q000201:enzymology; D007074:Immunoglobulin G / Q000378:metabolism*; D007930:Leucine / Q000378:metabolism; D012510:Sarcoma 180 / Q000201:enzymology / Q000276:immunology* / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000276:immunology / Q000378:metabolism*
D000912:Antibodies, Neoplasm; D007074:Immunoglobulin G; D000254:Sodium-Potassium-Exchanging ATPase; D007930:Leucine