Additivity of lytic activities for mutant lysozymes

Abstract: We constructed various Iysozyme mutants and their addition mutants. Each mutation, Asn27Asp (activity 84%), Lys33Asn (130%), Ser36Thr (175%), SerS0Thr (140%) and Trp62Tyr (130%) was respectively added to the double mutant Aspl01Gly/Gly102Pro (225%). As the result of the additive mutations, activities of these triple mutants were 217%, 318%, 367%, 273% and 264% of wild type, respectively. These results show that the additivity is held in lytic activity whose mechanism is complex.