Purification and characterization of prophenoloxidase from the haemolymph of Locusta migratoria
Purification and characterization of prophenoloxidase from the haemolymph of Locusta migratoria
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飞蝗血淋巴中酚氧化酶原的纯化及表征
DOI：
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发表时间：
1996
期刊：
影响因子：
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通讯作者：
M. Brehélin
中科院分区：
文献类型：
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作者：
A. Cherqui;B. Duvic;M. Brehélin
从东亚飞蝗（Locusta migratoria）血浆中分离纯化了酚氧化酶原（proPO）。这是在三个步骤中实现的（在5300上进行凝胶过滤，在QMA Memsep上进行阴离子交换，以及在蓝色Trisacryl上进行亲和层析），而不使用抗凝剂缓冲液或抑制剂。天然蛋白质的表观分子量为250 kDa，通过凝胶过滤测定，可能由三个81 kDa的非共价缔合亚基组成。发现其氨基酸组成与Bombyx mori proPO非常相似。纯化的刺槐酚氧化酶原能被α-糜蛋白酶转化为酚氧化酶（PO）。以左旋多巴为底物，测定Kin和Vmax分别为1.5mM和5 μM/s。© 1996 Wiley-Liss公司。
Prophenoloxidase (proPO) was purified from plasma of the locust, Locusta migratoria. This was achieved in three steps (gel filtration on 5300, anion exchange on QMA Memsep, and affinity chromatography on blue Trisacryl) without the use of anticoagulant buffer or inhibitors. The native protein had an apparent molecular mass of 250 kDa as determined by gel filtration and was likely composed of three non-covalently associated subunits of 81 kDa. Its amino acid composition was found to be very similar to that of Bombyx mori proPO. Purified locust proPO could be converted into phenoloxidase (PO) by α-chymotrypsin. Using L-dopa as substrate, Kin and Vmax were determined to be 1.5 mM and 5 μM/s, respectively. © 1996 Wiley-Liss, Inc.
DOI：
10.1073/pnas.92.17.7764
发表时间：
1995-08-15
影响因子：
11.1
作者：
HALL, M;SCOTT, T;LAW, JH
通讯作者：
LAW, JH