title: Detection of Tsh protein mucinolytic activity by SDS-PAGE.
abstract: The temperature-sensitive hemagglutinin (Tsh, 140 kDa) produced by Escherichia coli is cleaved into a fragment (106 kDa) containing mucinase activity, and an agglutinin fragment (33 kDa). By incorporating mucins into SDS-PAGE gels stained by Schiff's periodic acid, we could simultaneously detect about 0.5 microg of mucinase activity and the fragment molecular mass.
authors.affiliation: Universidade Estadual de Londrina, Depto de Microbiologia-CCB, Campus Universitário, Caixa Postal 6001, 86051-970-Londrina, Pr, Brazil. cmokino@sercomtel.com.br
authors.forename: Renata K T
authors.initials: RK
authors.lastname: Kobayashi
authors.forename: Luis Carlos J
authors.initials: LC
authors.lastname: Gaziri
authors.forename: Emerson J
authors.initials: EJ
authors.lastname: Venancio
authors.forename: Marilda C
authors.initials: MC
authors.lastname: Vidotto
mesh_terms: D018830:Adhesins, Escherichia coli / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D004926:Escherichia coli / Q000378:metabolism*; D006388:Hemagglutinins / Q000378:metabolism; D009077:Mucins / Q000378:metabolism; D011133:Polysaccharide-Lyases / Q000378:metabolism*
chemical_list: D018830:Adhesins, Escherichia coli; D006388:Hemagglutinins; D009077:Mucins; C112027:tsh protein, E coli; D011133:Polysaccharide-Lyases; C100002:hyaluronate lyase