ACTIVITY OF LACTIC DEHYDROGENASE IN REVERSE MICELLES FORMED BY DODECYLAMMONIUM IN CYCLOHEXANE
乳酸脱氨酶DAB－环己烷反胶束溶液中的活性

The enzymatic activity of rabbit muscle lactic dehydrogenase (LDH) solubillized in reverse micelles formed by dodecylammonium butyrare (DAB) in cyclohexane has ho investigated. It was found that the activity of LDH increases with the increase of solubilized water content. At high water content in 0.1mol·1-1 DAN cyclohexane solution, the turnover number of LDH in reverse micelles was close to that in aqueous solution. The activity of LDH increased with the decrease of DAB conathon at constant wo (=H2O]/DAB]).