Evidence of a Heparin-Binding Protein in the Plasma of the Slipper Oyster, Crassostrea iredalei

被引：0
|
作者：
Zamani, A. I. [1 ]
Nadirah, M. [2 ]
Amiza, M. A. [3 ]
Najiah, M. [1 ]
机构：
[1] Univ Malaysia Terengganu, Dept Aquaculture Sci, Kuala Terengganu 21030, Terengganu, Malaysia
[2] Univ Malaysia Terengganu, Fac Fisheries & Aquaind, Dept Fisheries Sci, Kuala Terengganu 21030, Terengganu, Malaysia
[3] Univ Malaysia Terengganu, Fac Agrotechnol & Food Sci, Dept Food Sci, Kuala Terengganu 21030, Terengganu, Malaysia
来源：
JOURNAL OF ANIMAL AND VETERINARY ADVANCES | 2012年 / 11卷 / 22期
关键词：
Heparin-Binding Protein (HBP); Crassostrea iredalei; 2D-electrophoresis; proPhenoloxidase-activating (proPO) system; Malaysia; PROPHENOLOXIDASE-ACTIVATING SYSTEM; CRAYFISH PACIFASTACUS-LENIUSCULUS; PHENOLOXIDASE ACTIVITY; PACIFIC OYSTER; BETA-1,3-GLUCAN-BINDING PROTEIN; SULFATED GLYCOSAMINOGLYCANS; INVERTEBRATE IMMUNITY; SACCOSTREA-GLOMERATA; RECOGNITION PROTEIN; PENAEUS-VANNAMEI;
D O I：
暂无
中图分类号：
S85 [动物医学（兽医学）];
学科分类号：
0906 ;
摘要：
Recognition proteins play an important role in the immunodefense system of invertebrates. The haemolymph of the Slipper oyster, Crassostrea iredalei, 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 beta-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 C. gigas.
引用
收藏
页码：4147 / 4155
页数：9
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