Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate.

摘要: Abstract Chaperonin isolated from Thermus thermophilus is stable up to 80 degrees C. Taking advantage of this heat stability, we have studied the effects chaperonin on denaturation several relatively labile enzymes. When enzymes are incubated at their denaturating temperatures, presence T. in solution has little effect rate apparent inactivation enzyme. However, not irreversible since most activity recovered when shifted second incubation a moderate temperature with concomitant addition MgATP. omitted solution, no recovery observed. Recovery also dependent MgATP and 50% attained 5 microM added after starting denaturing temperature, becomes poorer as delay increases. The critical which occurs elevated 8-15 C by inclusion solution. stability captured proteins chaperonin, assessed retention ability resume productive folding under optimal conditions, measured more accurately using chemically produced intermediate-chaperonin complexes. lost about 78 being irrespective variable individual These results indicate that during assume common structure recognizable chaperonin. Once protein it retains even exposure otherwise high temperature. Its seems be limited solely