The analysis by isoelectric focusing of the secretion fluid (AGF) of the female accessory glands of Ceratitis capitata has shown the presence of seven major protein fractions and two β-N-acetylhexosaminidase isoenzymes, HEX 1 and HEX 2, focalizing at pH 4.75 and 5.25, respectively. The two isoenzymes have the same molecular weight (69 kDa) but a different hydrolytic activity against and galactopyranoside, and a pH optimum of 4 at 37°C. AGF β-N-acetylhexosaminidase activity is most stable at pH values between 5 and 8. At neutral pH a rapid loss of activity is observed at temperatures higher than 50°C. Preliminary assays, carried out using chitin as substrate, indicate the presence in the secretion of an endochitinase activity not bound to the β-N-acetylhexosaminidase isoenzymes. The enzymatic modifications of specific lectin binding sites on the surface of gametic cells is most probably one of the necessary steps preceding fertilization.
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|Titolo:||ß-N-acetylhexosaminidases in the secretion of the female reproductive accessory glands of Ceratitis capitata (Diptera)|
|Citazione:||Marchini, D., L., B., & R., D. (1989). ß-N-acetylhexosaminidases in the secretion of the female reproductive accessory glands of Ceratitis capitata (Diptera). INSECT BIOCHEMISTRY, 19(6), 549-555.|
|Appare nelle tipologie:||1.1 Articolo in rivista|