Chitinase and beta-N-acetylglycosaminidase in the digestive juice of Helix pomatia

A beta-N-acetylglucosaminidase from Helix pomatia digestive juice was separated and partly purified by gel chromatography. The optimal pH for the degradation of p-nitrophenyl-N-acetyl-beta-D-glucosaminide was 3.4. The molecular weight was around 160 000 and the pI = 4.95. In the same gel chromatogra...

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Bibliographic Details
Published in:	Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry Vol. 30 B; no. 9; p. 889
Main Authors:	Lundblad, G, Elander, M, Lind, J
Format:	Journal Article
Language:	English
Published:	Denmark 1976
Subjects:	Acetylglucosaminidase - analysis Animals Chitinases - analysis Chromatography, Gel Gastric Juice - enzymology Helix (Snails) - enzymology Hexosaminidases - analysis Hydrogen-Ion Concentration Isoelectric Focusing Molecular Weight Snails - enzymology
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Summary:	A beta-N-acetylglucosaminidase from Helix pomatia digestive juice was separated and partly purified by gel chromatography. The optimal pH for the degradation of p-nitrophenyl-N-acetyl-beta-D-glucosaminide was 3.4. The molecular weight was around 160 000 and the pI = 4.95. In the same gel chromatography run two chitinase active peaks were also obtained. These chitinase active peaks were also obtained. These chitinases, with molecular weights around 26 000 and 13 000, had somewhat different pH activity curves with optima at 4.2 and 4.3. By isoelectric focusing the first peak with molecular weight around 26 000 was divided in two chitinase active regions with pI at 5.7 and 3.5. The second peak with molecular weight around 13 000 had a pI at 7.3.
ISSN:	0302-4369