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Catalytic properties and polymorphism of serine endopeptidases from the midgut gland of the brown shrimp Crangon crangon (Decapoda, Caridea)
Saborowski, R.; Schatte, J.; Giménez, L. (2012). Catalytic properties and polymorphism of serine endopeptidases from the midgut gland of the brown shrimp Crangon crangon (Decapoda, Caridea). Mar. Biol. (Berl.) 159(5): 1107-1118. http://hdl.handle.net/10.1007/s00227-012-1890-0
In: Marine Biology. Springer: Heidelberg; Berlin. ISSN 0025-3162, more
Peer reviewed article  

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Keyword
    Marine

Authors  Top 
  • Saborowski, R.
  • Schatte, J.
  • Giménez, L.

Abstract
    The brown shrimp Crangon crangon is a key species in the coastal areas of the North Sea. It constitutes a significant food source for fishes. Simultaneously, it is an important predator on a wide range of invertebrates. C. crangon shows a variety of digestive enzymes that allow to utilizing a wide range of food items. The initial step of alimentary protein digestion, that is the degradation into peptides, is facilitated by set of endopeptidases which are expressed by the midgut gland. In crustaceans, these endopeptidases are often dominated by serine proteinases. C. crangon, however, predominantly express cysteine proteinases, while only some specimens show a highly variable pattern of serine proteinases. The composition of these serine endopeptidases was investigated using liquid chromatography, substrate gel electrophoresis and inhibitor assays. Distinctly elevated activities were present only in about 10% of the samples. When activity was detected, two peaks, one with tryptic activity and the other one with chymotryptic activity, could be separated by anionic exchange chromatography. Moreover, specimens with elevated tryptic activities often showed highly polymorphic patterns of endopeptidases after electrophoretic separation. Overall, 30 different bands of endopeptidases were identified. There was no similarity between animals from the same sampling sites, neither between animals of similar size, weight or nutritive state. The polymorphism of proteinase from the midgut gland seems to reflect the high adaptive potential of this species to variable trophic conditions in a continuously changing environment.

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