Purification of hemocyanin from white shrimp (Penaeus vannamei Boone) by immobilized metal affinity chromatography

被引：25

作者：

FigueroaSoto, CG ^{[1
]}

delaBarca, AMC ^{[1
]}

VazquezMoreno, L ^{[1
]}

HigueraCiapara, I ^{[1
]}

YepizPlascencia, G ^{[1
]}

机构：

[1] CTR INVEST ALIMENTAC & DESARROLLO,HERMOSILLO 83000,SONORA,MEXICO

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1997年 / 117卷 / 02期

关键词：

affinity; antibodies; copper; crustacea; shrimp hemocyanin; hemolymph; metal affinity;

D O I：

10.1016/S0305-0491(96)00321-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Hemocyanin (He) was isolated from white shrimp (Penaeus vannamei Boone) plasma by density gradient ultracentrifugation and immobilized metal affinity chromatography. He was contained in the subnatant high density fraction and was adsorbed by an iminodiacetic acid (Ni-IDA) column that bound He and apohemocyanin. He molecular weight was estimated by pore limiting electrophoresis as 400 kDa. It is composed of two subunits of approximately 75 and 82 kDa. This 400-kDa protein contained copper and was detected by antibodies raised against the purified subunits. Isoelectric points of the affinity purified native protein were 4.8 and 4.9. Presence of covalently bound carbohydrates in both subunits was detected by biotinylated lectins and avidin-horseradish peroxidase. (C) 1997 Elsevier Science Inc.

引用

页码：203 / 208

页数：6

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