One of two diapause hormones (DH-A) was studied. DH-A was stable to acids, bases (except to 1·0 N NaOH), acylation agents and periodate oxidation. The hormonal activity was quickly lost by trypsin as well as by non-specific proteolytic enzymes but slowly or hardly at all by α-chymotrypsin and carboxypeptidase A. The hormone contains 14 kinds of amino acids and 2 kinds of amino sugars. The amino sugars appear not to be essential for the hormonal activity. © 1975.
Isobe, M., Hasegawa, K., & Goto, T. (1975). Further characterization of the silkworm diapause hormone A. Journal of Insect Physiology, 21(12), 1917–1920. https://doi.org/10.1016/0022-1910(75)90223-1