Further characterization of the silkworm diapause hormone A

  • Isobe M
  • Hasegawa K
  • Goto T
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Abstract

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.

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Authors

  • Minoru Isobe

  • Kinsaku Hasegawa

  • Toshio Goto

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