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Trehalose catabolism enzymes in L3 and L4 larvae of Anisakis simplex.
J Parasitol 2007; 93(6):1291-4JP

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 LA 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.

Authors+Show Affiliations

University Warmia and Mazury, Faculty of Biology, Department of Biochemistry, Olsztyn 10-957, Oczapowskiego 1A, Poland. ela.lopienska@uwm.edu.plNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18314671

Citation

Lopieńska-Biernat, E, et al. "Trehalose Catabolism Enzymes in L3 and L4 Larvae of Anisakis Simplex." The Journal of Parasitology, vol. 93, no. 6, 2007, pp. 1291-4.
Lopieńska-Biernat E, Zółtowska K, Rokicki J. Trehalose catabolism enzymes in L3 and L4 larvae of Anisakis simplex. J Parasitol. 2007;93(6):1291-4.
Lopieńska-Biernat, E., Zółtowska, K., & Rokicki, J. (2007). Trehalose catabolism enzymes in L3 and L4 larvae of Anisakis simplex. The Journal of Parasitology, 93(6), pp. 1291-4. doi:10.1645/GE-906.1.
Lopieńska-Biernat E, Zółtowska K, Rokicki J. Trehalose Catabolism Enzymes in L3 and L4 Larvae of Anisakis Simplex. J Parasitol. 2007;93(6):1291-4. PubMed PMID: 18314671.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Trehalose catabolism enzymes in L3 and L4 larvae of Anisakis simplex. AU - Lopieńska-Biernat,E, AU - Zółtowska,K, AU - Rokicki,J, PY - 2008/3/5/pubmed PY - 2008/3/11/medline PY - 2008/3/5/entrez SP - 1291 EP - 4 JF - The Journal of parasitology JO - J. Parasitol. VL - 93 IS - 6 N2 - 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 LA 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. SN - 0022-3395 UR - https://www.unboundmedicine.com/medline/citation/18314671/Trehalose_catabolism_enzymes_in_L3_and_L4_larvae_of_Anisakis_simplex_ L2 - http://www.journalofparasitology.org/doi/10.1645/GE-906.1?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -