@article{MAKHILLJAVA201211223863,
    title = {Evidence of a Heparin-Binding Protein in the Plasma of the Slipper Oyster, <I>Crassostrea iredalei</I>},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {11},
    number = {22},
    pages = {4147-4155},
    year = {2012},
    issn = {1680-5593},
    doi = {javaa.2012.4147.4155},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2012.4147.4155},
    author = {M.,A.I.,M. and},
    keywords = {Heparin-Binding Protein (HBP),Crassostrea iredalei,2D-electrophoresis,proPhenoloxidase-activating (proPO) system,Malaysia},
    abstract = {Recognition proteins play an important role in the immunodefense 
  system of invertebrates. The haemolymph of the Slipper oyster, <I>Crassostrea 
  iredalei</I>, contains a heparin-binding protein with a molecular weight of 
  35 kDa as determined by SDS-PAGE analysis. The protein was purified using column 
  chromatography. This binding protein possesses a serine protease activity thus 
  it is capable of activating the prophenoloxidase-activating (proPO) system. 
  However, the protein lacks &#946;-1,3-glucanase activity. Using rabbit antiserum 
  against the isolated protein in immunodiffusion and immunoblotting assays it 
  produced a single precipitant and a single band, respectively. However, N-terminal 
  amino acid sequence of BGBP: Threonine-Alanine-Arginine-Asparagine-Glutamic 
  acid-Alanine-Asparagine-Valine was similar to Cavortin (AAT44352) and extracellular 
  superoxide dismutase (AAY60161) from <I>C. gigas</I>.}
    }