Immunochemical comparison of L-asparaginases from Serratia marcescens and Escherichia coli.
Immunochemical properties of l-asparaginases from Serratia marcescens and Escherichia coli were compared by means of quantitative precipitin reactions and quantitative microcomplement-fixation reactions employing homologous and heterologous antisera. The enzyme preparations used in these tests produced one arc of precipitate upon immunoelectrophoresis. According to our results with the precipitin and micro-complement fixation reactions, both enzymes are related immunochemically. On the basis of these tests, distinct structural differences exist between the two enzymes. From results with the micro-complement fixation test, we estimated that the two enzymes could differ by 10 to 15 amino acid residues.
D000641:Ammonia / Q000096:biosynthesis; D000818:Animals; D000937:Antigen-Antibody Reactions; D001215:Asparaginase / Q000378:metabolism; D003168:Complement Fixation Tests; D003429:Cross Reactions; D004926:Escherichia coli / Q000201:enzymology* / Q000276:immunology; D007106:Immune Sera; D007120:Immunochemistry; D007122:Immunoelectrophoresis; D011233:Precipitin Tests; D011817:Rabbits; D012706:Serratia marcescens / Q000201:enzymology* / Q000276:immunology; D013045:Species Specificity; D013053:Spectrophotometry
D007106:Immune Sera; D000641:Ammonia; D001215:Asparaginase