Androgenic gland hormone (AGH) is known to be responsible for sex different
iation in crustaceans. The amino acid sequence of AGH-active fraction purif
ied from androgenic glands of the terrestrial isopod Armadillidium vulgare
was determined by immunoprecipitation employing three types of antibodies r
aised against differing parts of the amino acid sequence deduced from the p
utative AGH cDNA sequence. As all antibodies adsorbed AGH activity, it was
confirmed that the sequence examined was that of AGH. The affinity of AGH t
o certain lectins indicated that AGH possesses a carbohydrate moiety, which
is in agreement with the observation that AGH possesses an N-glycosylation
consensus sequence. (C) 2001 Elsevier Science Inc. All rights reserved.