KINETICS OF EXPRESSION OF LUCIFERASE GENES FROM THE FIREFLIES PHOTINUS-PYRALIS AND LUCIOLA-MINGRELICA IN ESCHERICHIA-COLI .2. ROLE OF PH INTHE BIOSYNTHESIS OF PROTEINS AND THEIR TRANSFORMATION INTO ACTIVE CONFORMERS

The kinetics of expression of firefly luciferase genes from Photinus p yralis and Luciola mingrelica was studied in E. coli CA cells transfor med with plasmids pME61 and pJG lambda, respectively, carrying the the rmally inducible lambda P-R promoter, under conditions of shifted pH w hich increased the enzymatic activity. The maximal levels of luciferas e from Ph. pyralis and L. mingrelica indicated by electrophoresis in 1 2% polyacrylamide gels in the presence of sodium dodecyl sulfate was 5 .3 and 4.9%, respectively, of the total cell protein with the external pH shifted from 7.5 to 9.0; the corresponding levels were 4.7 and 4.5 % with the internal pH shifted to 8.5. There was a correlation between enzyme activation and changes in external or internal pH.