Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus.

@article{Wang2001PropertiesOT,
  title={Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus.},
  author={Rui Wang and So Young Lee and Lage Cerenius and Kenneth S{\"o}derh{\"a}ll},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 4},
  pages={
          895-902
        }
}
The prophenoloxidase activating enzyme (ppA), a serine proteinase catalyzing the conversion of prophenoloxidase to an active phenoloxidase, has a molecular mass of about 36 kDa in its active form. This protein was cloned from a blood cell cDNA library and its corresponding cDNA of 1736 base pairs encodes a zymogenic protein (proppA) of 468 amino acids. An antibody raised against a synthetic peptide derived from a region of the cDNA sequence could efficiently inhibit the beta-1,3-glucan… CONTINUE READING
Highly Cited
This paper has 105 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 45 extracted citations

Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology • 2009
View 4 Excerpts
Highly Influenced

Recent advances in the innate immunity of invertebrate animals.

Journal of biochemistry and molecular biology • 2005
View 3 Excerpts
Highly Influenced

106 Citations

0510'01'04'08'12'16
Citations per Year
Semantic Scholar estimates that this publication has 106 citations based on the available data.

See our FAQ for additional information.