Premium
Characterisation of a glycoprotein in oviductal fluid by two‐dimensional electrophoresis and lectin binding to protein gel blots
Author(s) -
Sutton Rosemary,
Wallace Alan L. C.,
Nancarrow Colin D.
Publication year - 1985
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150061010
Subject(s) - fucose , sialic acid , glycoprotein , isoelectric point , lectin , blot , biochemistry , chemistry , isoelectric focusing , gel electrophoresis , mannose , concanavalin a , protein subunit , molecular mass , chromatography , galactose , microbiology and biotechnology , biology , in vitro , enzyme , gene
Two‐dimensional electrophoresis and Western blotting with lectins were used to provide information about a glycoprotein without requiring its previous purification. The oestrus‐associated glycoprotein from ovine oviductal fluid has an isoelectric point of 4.7 and a subunit molecular weight ( M r ) range of 70 000–90 000. Under non‐denaturing conditions, it is present as a high molecular weight aggregate or polymer although at low pH some monomer is also detected. The surface carbohydrate on this protein includes fucose, galactose and N‐acetyl galactosamine residues but not glucose, mannose or sialic acid.