胎盘和血清催产素酶亚基在电泳并转印至硝酸纤维素膜后与凝集素的结合。

Lectin binding of subunits of placental and serum oxytocinase after electrophoresis and transblotting to nitrocellulose.

Lalu K, Lampelo S, Vanha-Perttula T

Department of Anatomy, University of Kuopio, Finland.

Int J Biochem. 1988;20(9):1009-14. doi: 10.1016/0020-711x(88)90189-9.

Abstract

Oxytocinase enzymes were purified from maternal serum and human placenta, run by SDS-PAGE and transferred onto nitrocellulose. Both enzymes were homogeneous in protein staining with Mr of 145,000. 2. Both serum and placental oxytocinases bound concanavalin A (Con A), limax flavus agglutinin (LFA) and wheat germ agglutinin (WGA). The WGA-binding of the placental enzyme was more strongly inhibited by 0.2 M N-acetylglucosamine than that of the serum enzyme which may indicate a higher sialic acid content in the serum enzyme. 3. Neuraminidase treatment did not affect the binding of Con A but decreased the binding of WGA to serum and placental enzymes. Serum enzyme showed a pl 4.7 on isoelectric focusing.

摘要

从母体血清和人胎盘中纯化催产素酶，经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分离后转移至硝酸纤维素膜上。两种酶在蛋白质染色中均呈均一性，分子量为145,000。2. 血清和胎盘催产素酶均能结合伴刀豆球蛋白A（Con A）、黄斑海蜗牛凝集素（LFA）和麦胚凝集素（WGA）。0.2M N-乙酰葡糖胺对胎盘酶与WGA结合的抑制作用比对血清酶的更强，这可能表明血清酶中唾液酸含量更高。3. 神经氨酸酶处理不影响Con A的结合，但会降低WGA与血清和胎盘酶的结合。血清酶在等电聚焦时显示等电点为4.7。