title: Lectin binding of subunits of placental and serum oxytocinase after electrophoresis and transblotting to nitrocellulose.
abstract: 1. 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.
authors.affiliation: Department of Anatomy, University of Kuopio, Finland.
authors.forename: K
authors.initials: K
authors.lastname: Lalu
authors.forename: S
authors.initials: S
authors.lastname: Lampelo
authors.forename: T
authors.initials: T
authors.lastname: Vanha-Perttula
mesh_terms: D000626:Aminopeptidases / Q000378:metabolism*; D003101:Collodion; D003208:Concanavalin A; D010122:Cystinyl Aminopeptidase / Q000378:metabolism*; D004586:Electrophoresis; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
chemical_list: D003208:Concanavalin A; D003101:Collodion; D000626:Aminopeptidases; D010122:Cystinyl Aminopeptidase