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Effective pretreatment by cysteine proteinase inhibitor for improved analysis of protein components of trematodes on SDS-PAGE

Published online by Cambridge University Press:  05 June 2009

M. Itoh ,
S. Sato ,
A. Moriyama  and
M. Sasaki
M. Itoh
Affiliation:
Department of Medical Zoology, Nagoya City University Medical School, Kawasumi, Mizuho, Nagoya, 467 Japan
S. Sato
Affiliation:
Department of Medical Zoology, Nagoya City University Medical School, Kawasumi, Mizuho, Nagoya, 467 Japan
A. Moriyama
Affiliation:
Department of Biochemistry, Nagoya City University Medical School, Kawasumi, Mizuho, Nagoya, 467 Japan
M. Sasaki
Affiliation:
Department of Biochemistry, Nagoya City University Medical School, Kawasumi, Mizuho, Nagoya, 467 Japan
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Abstract

Since Fasciola sp. contained proteolytic enzyme(s), it was confirmed that degradation took place in protein components in extracts of the liver flukes, which resulted in lack of clarity of sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Degradation was shown to occur mostly during a heating process of the extract samples. The proteolytic activity in the extracts was completely blocked and electrophoretic patterns were improved only by the use of cysteine proteinase inhibitor N-[N-(L-3-trans-carboxyoxiran-2-carbonyl)-L-leucyl]-agmatine (E-64). Great improvement was also noted in electrophoretic patterns of the extracts of other trematodes, such as Paragonimus westermani, P. miyazakii and Clonorchis sinensis, when their extracts were treated with E-64.

Keywords

trematodescysteine proteinasecysteine proteinase inhibitorsgel electrophoresisFasciolaClonorchis sinensisParagonimus westermaniParagonimus miyazakii
Type
Research Article
Information
Journal of Helminthology , Volume 64 , Issue 3 , September 1990 , pp. 175 - 179
Copyright
Copyright © Cambridge University Press 1990

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References

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