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

页码：4147 / 4155

页数：9

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