Localization of a chymotrypsin-like protease to the perivitelline space of Xenopus laevis eggs.
A chymotrypsin-like protease is released from Xenopus laevis eggs at activation and is involved in conversion of the vitelline envelope to the fertilization envelope. To localize this enzyme in unactivated and activated eggs, we used the synthetic peptide substrate succinylalanylalanylprolylphenylalanyl-4-methoxy-2-naphthylamide whose product can be visualized using transmission electron microscopy. Protease product was localized within the perivitelline space of unactivated eggs, appearing as strings of beads. No protease activity was detected in activated eggs, which is consistent with the observation that the protease is released from the egg at activation.
Lindsay
L L
LL
Department of Biochemistry and Biophysics, University of California, Davis 95616.
Larabell
C A
CA
Hedrick
J L
JL
D000818:Animals; D002462:Cell Membrane / Q000648:ultrastructure; D002918:Chymotrypsin / Q000032:analysis*; D010450:Endopeptidases / Q000032:analysis*; D005260:Female; D008297:Male; D010063:Ovum / Q000201:enzymology* / Q000648:ultrastructure; D013084:Sperm-Ovum Interactions; D014817:Vitelline Membrane / Q000201:enzymology* / Q000648:ultrastructure; D014982:Xenopus laevis
D010450:Endopeptidases; D002918:Chymotrypsin