title: Amphibian embryo protease inhibitor. III. Binding studies on the trypsin inhibitor and properties of its yolk-bound form.
abstract: Amphibian embryo trypsin inhibitor (ATI) is shown to be a temporary inhibitor in which full trypsin activity can eventually be restored. Lineweaver-Burk plots and other binding data indicate a reversible change from competitive to non-competitive inhibition during incubation of enzyme with inhibitor in the absence of substrate. The inhibitor is active while sequestered in the yolk, and the sequestered inhibitor co-purifies with lipovitellin when the yolk is fractionated. It is further demonstrated that the inhibitor slowly leaches from the yolk in a soluble form, and it is suggested that this leakage is the result of a negative feedback controlled proteolysis within the yolk. Possible interactions between ATI and endogenous trypsin-like proteases are discussed with particular regard to the potential involvement of those materials in the control of certain developmental events; notably melanogenesis.
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D004527:Egg Proteins / Q000378:metabolism; D004530:Egg Yolk; D005260:Female; D007700:Kinetics; D010063:Ovum / Q000378:metabolism*; D014106:Tosylarginine Methyl Ester / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000378:metabolism*
chemical_list: D004527:Egg Proteins; D014361:Trypsin Inhibitors; D014106:Tosylarginine Methyl Ester; D014357:Trypsin