[Study of intracellular localization of the proteolytic enzyme complex and its protein inhibitors in bombyx grain].

Intracellular localization of serine, cysteine and aspartate proteases, as well as their protein inhibitors, in bombyx grain in the postdiapause period of embryogenesis has been studied. Proteolytic activity of aspartate and cysteine proteases was found in lysosomal, mitochondrial, and nuclear fractions of grains. Serine protease activity was not observed in subcellular fractions of grains of the fourth day of postdiapause development.

[Proteolytic enzymes as markers of productivity and heterosis of silkworm].

A positive correlation between the activity level of cysteine proteinases in developing eggs of common silkworm moth (Bombyx mori L.), on the one hand, and a set of commercial characteristics, on the other, was found. This allows the determination of cysteine proteinase activities (pH optima of 3.

[A study of the complex of proteolytic enzymes and their protein inhibitors in embryogenesis of the silkworm].

We studied changes in the activities of serin, thiol, and aspartyl proteinases and their protein inhibitors during embryogenesis of the silkworm. The dynamics of activities of the protein inhibitors and specific proteinases were interrelated, thus providing for coordination and fine regulation of functioning of the proteolytic complex of enzymes during embryogenesis. Possible functions of peptidohydrolases and their protein inhibitors in the silkworm are discussed.