Urch U A, Hedrick J L
Department of Biochemistry and Biophysics, University of California, Davis 95616.
J Supramol Struct Cell Biochem. 1981;15(2):111-7. doi: 10.1002/jsscb.1981.380150202.
Hatching in the amphibian Xenopus laevis involves release of an embryo-secreted hatching enzyme, a protease, which weakens the envelope surrounding the embryo. The envelope is not totally solubilized, which infers that only selected envelope components are hydrolyzed by the enzyme. The susceptibility of the glycoprotein components composing the envelope to hydrolysis by the hatching enzyme was investigated. Isolated envelopes in various physical states, ie, particulate and solubilized, were treated with the hatching enzyme, and the resulting envelope hydrolysis products were characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The susceptibility of the envelope components to proteolysis was not a function of the state of the envelope. The envelope components most susceptible to proteolysis were the 125K and 118K components followed by the 60K and 71-77K components. These components are minor constituents of the envelope. The major constituents, 33K and 40K, were relatively resistant to hydrolysis by the hatching enzyme. From these observations, we infer that the envelope components hydrolyzed are components that link or bind together the major structural elements of the envelope, eg, the 33K and 40K components. Selective destruction of the components required for maintaining the structural integrity of the envelope, eg, the "nuts and bolts" of the structure, permits a weakening of the envelope that allows the embryo to hatch without having to destroy totally (hydrolyze) the envelope.
