Localization of the proenzyme form of the vitellin-processing protease in Blattella germanica by affinity-purified antibodies.
During Blattella germanica embryo development, the nutritive yolk protein vitellin is processed by a cysteine protease, which is activated proteolytically from a proprotease during acidification of yolk granules. A murine polyclonal antiserum was generated with the purified proprotease as the immunogen. The antiserum was made monospecific to proprotease by subtractive affinity chromatography using proprotease-free yolk proteins as ligand. The purified antibodies were employed to investigate the temporal and spatial expression of the proprotease during vitellogenesis and embryo development. Anti-proprotease-reactive peptides appeared in extracts of fat bodies and ovarian follicles of post-mating females, but not in fat bodies of males or the fat bodies or follicles of unmated females, suggesting that the proprotease is synthesized extraovarially. Use of the antibodies was extended to monitor the kinetics of proprotease disappearance during early embryo development.
Liu
X
X
Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst 01003, USA.
Nordin
J H
JH
D000818:Animals; D000906:Antibodies / Q000302:isolation & purification; D002846:Chromatography, Affinity; D003058:Cockroaches / Q000196:embryology / Q000201:enzymology*; D004527:Egg Proteins / Q000302:isolation & purification; D004625:Embryo, Nonmammalian / Q000502:physiology; D004792:Enzyme Precursors / Q000032:analysis*; D051379:Mice; D008807:Mice, Inbred BALB C; D012697:Serine Endopeptidases / Q000032:analysis*
D000906:Antibodies; D004527:Egg Proteins; D004792:Enzyme Precursors; D012697:Serine Endopeptidases; C072296:vitellin-degrading protease