Hemocyanin from shrimp Litopenaeus vannamei shows hemolytic activity

Cloning and characterization of the hemocyanin gene of prawn Macrobrachium nipponense

“…As the main protein component of haemolymph, hemocyanin typically represents up to 90% of total amount of protein [1]. Except for its primary function as an oxygen-carrier, hemocyanin is a multi-functional protein involved in several physiological processes and immue defence such as phenoloxidase activity [2,3], hemolytic activity [4], anti-virus [5] and anti-bacteria [6]. The freshwater prawn Macrobrachium nipponense (M. nipponense) an economically important species, is a primary inland cultured species in China, Japan and Annam.…”

Enhanced resistance of Portunus trituberculatus to Vibrio alginolyticus by selective breeding

“…PO is thought to play an important role in the innate immune system of crustaceans (Söderhäll and Cerenius, 1998). Hemocyanin is an extracellular giant copper-containing protein found in the hemolymph of both mollusks and arthropods (Zhang et al, 2009). Hemocyanin and phenoloxidase are both copper-binding proteins involved in the immune system of a wide range of animal species (Lee et al, 2004).…”

Identification and agglutination properties of hemocyanin from the mud crab (Scylla serrata)

“…It has been documented that immune function of hemocyanins is conformation-or oligomer-dependent [16,25,37]. Other evidence indicates that the phenoloxidase activity of hemocyanin from the tarantula Eurypelma californicum is limited to just two of its seven subunits [16].…”

“…Minimum inhibitory concentration by saccharides (mM) or Omps (mg/ml) previous report indicated that L. vannamei hemocyanin might induce hemolysis as an oligomer (either dimer or trimer form) [25]. Therefore, it seemed possible that individual subunit of S. serrata hemocyanin might be active in inducing agglutination.…”

“…Protein purification using affinity chromatography has been previously described [25]. Briefly, rabbit anti-hemocyanin IgG (5 mg, prepared by immunization in the laboratory, purified by ammonium sulfate precipitation and ion-exchange chromatography), was covalently coupled to CNBr-activated sepharose 4B (0.5 ml) in carbonate buffer (0.5 M NaCl, 0.1 M NaHCO 3 , pH 8.3), and packed into a 2.0 ml syringe.…”