Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

TREHALOSE CATABOLISM ENZYMES IN L3 AND L4 LARVAE OF ANISAKIS SIMPLEX

TREHALOSE CATABOLISM ENZYMES IN L3 AND L4 LARVAE OF ANISAKIS SIMPLEX The presence of trehalase and trehalose phosphorylase in L3 and L4 larvae of Anisakis simplex was demonstrated. The activity of trehalase and trehalose phosphorylase in L3 larvae was 6 and 10 times higher, respectively, than in L4 larvae. This suggests that trehalose metabolism is more important for L3 than L4 larvae. Trehalases of L3 and L4 differ in their characteristics. The enzyme of L3 was present mainly in the lysosomes and cytosol, whereas in L4 the highest enzyme activity was measured in the lysosomal fraction. Trehalase activity was increased by 29% in L3 and 55% in L4 with the addition of Mg2+ (0.1 mmol). Tris inhibited trehalase in L3 larvae by 42% and in L4 by 25%. The enzymes differed in their reaction to EDTA, CaCl2, ZnCl2, and CH2ICOOH (all 0.1 mmol). High activity of trehalase from L3 larvae was measured within the pH range of 5.0 to 6.5, with an optimum pH of 6.1. The trehalase was a thermally tolerant enzyme from 25 C to 60 C. The enzyme lost half of its activity after preincubation without substrate above 75 C. The paper also discusses the similarities and differences in characteristics of trehalase from A. simplex larvae and presents the comparison to enzymes from other nematodes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Parasitology Allen Press

TREHALOSE CATABOLISM ENZYMES IN L3 AND L4 LARVAE OF ANISAKIS SIMPLEX

,; ,; ,
The Journal of Parasitology , Volume 93 (6): 4 – Dec 3, 2007
Download PDF
4 pages

Loading next page...
 
/lp/allen-press/trehalose-catabolism-enzymes-in-l3-and-l4-larvae-of-anisakis-simplex-BDOJu9MtKI

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Allen Press
Copyright
American Society of Parasitologists
Subject
BIOCHEMISTRY-PHYSIOLOGY
ISSN
0022-3395
eISSN
1937-2345
DOI
10.1645/GE-906.1
pmid
18314671
Publisher site
See Article on Publisher Site

Abstract

The presence of trehalase and trehalose phosphorylase in L3 and L4 larvae of Anisakis simplex was demonstrated. The activity of trehalase and trehalose phosphorylase in L3 larvae was 6 and 10 times higher, respectively, than in L4 larvae. This suggests that trehalose metabolism is more important for L3 than L4 larvae. Trehalases of L3 and L4 differ in their characteristics. The enzyme of L3 was present mainly in the lysosomes and cytosol, whereas in L4 the highest enzyme activity was measured in the lysosomal fraction. Trehalase activity was increased by 29% in L3 and 55% in L4 with the addition of Mg2+ (0.1 mmol). Tris inhibited trehalase in L3 larvae by 42% and in L4 by 25%. The enzymes differed in their reaction to EDTA, CaCl2, ZnCl2, and CH2ICOOH (all 0.1 mmol). High activity of trehalase from L3 larvae was measured within the pH range of 5.0 to 6.5, with an optimum pH of 6.1. The trehalase was a thermally tolerant enzyme from 25 C to 60 C. The enzyme lost half of its activity after preincubation without substrate above 75 C. The paper also discusses the similarities and differences in characteristics of trehalase from A. simplex larvae and presents the comparison to enzymes from other nematodes.

Journal

The Journal of Parasitology – Allen Press

Published: Dec 3, 2007

There are no references for this article.