GLYCOSYLATION AND ADHESIVENESS DIFFERENTIATE LARVAL CERATITIS-CAPITATA TYROSINASES

Citation
Nd. Charalambidis et al., GLYCOSYLATION AND ADHESIVENESS DIFFERENTIATE LARVAL CERATITIS-CAPITATA TYROSINASES, Archives of insect biochemistry and physiology, 27(4), 1994, pp. 235-248
Citations number
19
Categorie Soggetti
Entomology,Biology,Physiology
ISSN journal
07394462
Volume
27
Issue
4
Year of publication
1994
Pages
235 - 248
Database
ISI
SICI code
0739-4462(1994)27:4<235:GAADLC>2.0.ZU;2-3
Abstract
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 coli cell wall and hemocyte surface (unpublished data) while the gly cosylated form facilitated the secretion into serum.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.