An endonuclease, formerly purified from the digestive juice of silkworm larvae, is activated by Mg ions and attacks DNA and RNA, producing 5'-phosphoryl oligonucleotides.
Another nuclease was detected in the larval midgut tissue and purified about 4000 fold.
The two nucleases were comparatively studied with respect to their general properties, mutual relationship and possible metabolic conversion in relation to regulatory mechanisms of a nucleic acid digestive system in
Bombyx mori.
1. The digestive and midgut nucleases are optimally active at pH 10.3 and 9.5 respectively.
2. The midgut nuclease also attacks both DNA and RNA in the presence of Mg ions to give 5'-phosphoryl oligonucleotides.
3. Their approximate molecular weights as estimated by gel-filtration method are 22, 000 and 85, 000 respectively.
4. The two nucleases attack DNA by a single hit mechanism.
5. The two nucleases are immunologically similar.
6. The midgut nuclease is activated (probably by dissociation or digestion) by an unidentified activator partially purified from the digestive juice and is converted to an enzyme, the properties of which are closely similar to those of the digestive nuclease.
7. The activator is undialyzable and is inactivated by heating at 60°C for 10min.
8. These results suggest that the midgut nuclease is a low activity type proenzyme of the digestive nuclease.
9. Above-mentioned midgut nuclease appears to be identical to the pupal nuclease which was previously reported by Himeno
et al.
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