title: A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: tight binding to its natural substrate, egg envelope.
abstract: High choriolytic enzyme (HCE), a constituent protease of the hatching enzyme of the teleost, Oryzias latipes, swells its natural substrate, egg envelope (chorion) by hydrolyzing it partially. This enzyme was found to be bound tightly to the chorion when it exerted catalytic action. This was evidenced by the experimental results showing (i) that the turnover of this enzyme seemed to be hindered by the chorion, (ii) that the enzyme bound to the chorion could be recovered by washing with an alkaline medium, and (iii) that the bound enzyme could be quantified by radioimmunological estimation. The bound enzyme sustained its original activity and the binding between the enzyme and the chorion seems to be stoichiometric.
authors.affiliation: Life Science Institute, Sophia University, Tokyo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Yasumasu
authors.forename: S
authors.initials: S
authors.lastname: Katow
authors.forename: Y
authors.initials: Y
authors.lastname: Umino
authors.forename: I
authors.initials: I
authors.lastname: Iuchi
authors.forename: K
authors.initials: K
authors.lastname: Yamagami
mesh_terms: D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002823:Chorion / Q000378:metabolism*; D004527:Egg Proteins / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008666:Metalloendopeptidases / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D009990:Oryzias; D011863:Radioimmunoassay; D013379:Substrate Specificity
chemical_list: D004527:Egg Proteins; C015753:chorion proteins; D008666:Metalloendopeptidases; C024344:envelysin