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Thermal alterations of pyruvate kinases in the fish tapewormBothriocephalus acheilognathi, Yamaguti, 1934

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Abstract

The activity of pyruvate kinase was studied in extracts of the pseudophyllidean tapewormB. acheilognathi. Extracts were prepared from immature proglottides in the anterior region and mature proglottides in the posterior regions of the tapeworms. The optiomal pH was found to be 7.5 for both extracts. Protein contents were significantly lower, and specific activities of enzyme significantly higher, in extracts prepared from anterior regions. The apparent Michaelis constant (Km a) for phosphoenol pyruvate was measured in both extracts at temperatures ranging between 10°–40°C. Values were lower, at all temperatures, for anterior extracts. The differences were greatest between 15°–20°C and 35°–40°C. The evidence suggests that at least two forms of pyruvate kinase occur inBothriocephalus.

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Abbreviations

ADP:

adenosine diphosphate

FDP:

fructose-1,6-bisphosphate

PEP:

phosphoenol pyruvate

PEPCK:

phosphoenol pyruvate carboxykinase

PK:

pyruvate kinase

NADH:

micotinamide adenosine dinucleotide (reduced)

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Author notes

  1. M. Walkey

    Present address: School of Biological Sciences, Queen Mary College, Mile End Road, E1 4NS, London, UK

Authors and Affiliations

  1. Fish Diseases Research Unit, School of Veterinary Medicine, Bischofsholer Damm 15, 3000, Hannover 1, Federal Republic of Germany

    M. Walkey & W. Körting

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  1. M. Walkey
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  2. W. Körting
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Walkey, M., Körting, W. Thermal alterations of pyruvate kinases in the fish tapewormBothriocephalus acheilognathi, Yamaguti, 1934. Z. Parasitenkd. 71, 527–532 (1985). https://doi.org/10.1007/BF00928355

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  • DOI: https://doi.org/10.1007/BF00928355

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