A time-interval activation of esterase A4 by cold: Relation to the termination of embryonic diapause in the silkworm Bombyx mori

Abstract

The inactive esterase A4 (Ease A4) purified from the diapausing eggs of the silkworm, Bombyx mori, was chilled in vitro. The enzyme activity was very low during the early chilling period and it was suddenly elevated at a certain time of the chilling (2 weeks or less after chilling), depending upon when the chilling period began, and was followed by a rapid fall. The sudden elevation of the Ease A4 activity in vitro is equivalent to that observed in vivo and is coincident with the chilling period, the latter being indispensable for diapause termination. Data are also presented that suggest that the cold-induced activation of the Ease A4 may result from an autonomous structural change of the enzyme molecule which proceeds gradually in the cold.