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Purification and characterization of a b–glucan binding protein from the haemolymph of freshwater prawn Macrobrachium rosenbergii

b-glucan binding protein (bGBP), a pattern recognition protein was purified from the haemolymph of
freshwater prawn Macrobrachium rosenbergii by heparin affinity chromatography that showed a single
band in native gradient PAGE. The b-glucan binding property of the purified protein was confirmed
in a phenoloxidase (PO) assay, where addition of bGBP along with b-glucan increased the specific PO
activity compared with that of b-glucan alone. The molecular weight of the bGBP was found to be
~316 kDa on gel filtration chromatography. In SDS-PAGE, bGBP molecule was reduced to one
polypeptide chain of molecular weight ~113 kDa. Thus the bGBP in M. rosenbergii is possibly a homotrimeric molecule. The purified sample run on unreduced condition in SDS-PAGE also revealed a
similar size band (~113 kDa) and hence, the polypeptide chains of bGBP are held by non-covalent
interactions. The purified bGBP samples run in native PAGE was stained positively with alcian blue
for carbohydrates and Sudan black for lipids indicating the bGBP to be a glycolipoprotein. With rabbit
polyclonal anti-bGBP serum developed, an indirect ELISA was standardized and the normal bGBP concentration in adult M. rosenbergii serum was quantified to be ~2 mg mL
1. Furthermore, the applicability of the developed ELISA is discussed.

Keywords: Macrobrachium rosenbergii, b-glucan binding protein, affinity chromatography, ELISA

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Informasi Detail
Judul Seri
Aquaculture Research
No. Panggil
-
Penerbit
India : John Wiley & Sons Ltd,.,
Deskripsi Fisik
Aquaculture Research, 2015, 46, 95–104
Bahasa
English
ISBN/ISSN
doi:10.1111/are.1216
Klasifikasi
-
Tipe Isi
-
Tipe Media
-
Tipe Pembawa
-
Edisi
2015, 46, 95–104
Subjek
PERIKANAN
Info Detail Spesifik
-
Pernyataan Tanggungjawab
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