PURIFICATION AND CHARACTERIZATION OF HEMAGGLUTININ IN THE HEMOLYMPH OF THE SILKWORM, BOMBYX-MORI

被引：16

作者：

AMANAI, K ^{[1
]}

SAKURAI, S ^{[1
]}

OHTAKI, T ^{[1
]}

机构：

[1] KANAZAWA UNIV,FAC SCI,DEPT BIOL,1-1 MARUNOUCHI,KANAZAWA,ISHIKAWA 920,JAPAN

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 97卷 / 03期

关键词：

D O I：

10.1016/0305-0491(90)90146-K

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：

1. 1. Changes in haemagglutinating activity in haemolymph during 4th and 5th larval instars of Bombyx mori were stage specific. The activity increased in time concomitant with an increase in the secretory activity of prothoracic glands. 2. 2. The protein with haemagglutinating activity was purified by ammonium sulfate fractionation, gel-filtration on Sephacryl S-300 and affinity chromatography using either glucuronic acid or galacturonic acid as a ligand. 3. 3. Western blotting analysis using antibody raised against this protein revealed that Bombyx haemagglutinin is a tetramer composed of two different subunits with mol. wts of ca 88,000 and 90,000. © 1990.

引用

页码：471 / 476

页数：6

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