Nd. Charalambidis et al., GLYCOSYLATION AND ADHESIVENESS DIFFERENTIATE LARVAL CERATITIS-CAPITATA TYROSINASES, Archives of insect biochemistry and physiology, 27(4), 1994, pp. 235-248
Larval Ceratitis capitata phenoloxidases (POs) from hemocytes, serum,
integument, and fat body were analyzed. Two types of PO were recorded:
the tyrosinase type found in hemocytes, serum, integument, and fat bod
y and the laccase type found in integument. Tyrosinase from all larval
tissues and integumental laccase as well, showed similarity in molecu
lar weight (93 KDa), activation by Escherichia coli al 5 mM Ca2+, and
reactivity to antibodies raised against serum tyrosinase. However, the
enzymes differed with respect to their glycosylation and adhesiveness
. The serum and integumental enzyme forms contain concanavalin A react
ing material, whereas hemocyte and integumental tyrosinase(si are adhe
sive. These differences in enzyme forms, although not influencing thei
r substrate specificity, seem to give advantages to performing their f
unction, i.e., the adhesive enzyme form facilitates the adherence to E
. coli cell wall and hemocyte surface (unpublished data) while the gly
cosylated form facilitated the secretion into serum. (C) 1994 Wiley-Li
ss, Inc.