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Glycogen catabolism enzymes and protein fractions in the third and fourth larval stages of Anisakis simplex

Published online by Cambridge University Press:  01 March 2008

E. Łopieńska-Biernat ,
K. Żółtowska  and
J. Rokicki
E. Łopieńska-Biernat*
Affiliation:
Department of Biochemistry, Faculty of Biology, University Warmia and Mazury, Oczapowskiego 1A, Olsztyn 10-957, Poland
K. Żółtowska
Affiliation:
Department of Biochemistry, Faculty of Biology, University Warmia and Mazury, Oczapowskiego 1A, Olsztyn 10-957, Poland
J. Rokicki
Affiliation:
Department of Invertebrate Zoology, University of Gdansk, Pilsudskiego 46, Gdynia 81-378, Poland
*
*E-mail: ela.lopienska@uwm.edu.pl
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Abstract

Extracts of Anisakis simplex third (L3) and fourth (L4) larval stages were assayed for protein content and activity and properties of α-amylase, glucoamylase and glycogen phosphorylase. Protein content in L4 was twice that in L3. SDS–PAGE applied to both larval stages revealed 22 protein fractions in each, including five stage-specific fractions in each larval stage. The L3 extracts contained three amylase isoenzymes: α1, α2 and α3; their molecular weights were 64, 29 and 21 kDa, respectively. Only one amylase isoenzyme (64 kDa) was found in the L4 extracts. Glycogen in L3 was found to be broken down mostly by hydrolysis because of low glycogen phosphorylase activity. The α-amylase activity in L4 was higher than that in L3 by half and the glycogen phosphorylase activity was ten times higher. In addition, the same enzymes isolated from L3 and L4 were found to differ in their properties. These differences could be manifestations of metabolic adaptations of A. simplex larvae to host switch from fish (L3) to mammals (L4), i.e. adaptations to a new habitat.

Type
Research Papers
Information
Journal of Helminthology , Volume 82 , Issue 1 , March 2008 , pp. 45 - 51
Copyright
Copyright © Cambridge University Press 2007

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