Premium
Localization of the proenzyme form of the vitellin‐processing protease in Blattella germanica by affinity‐purified antibodies
Author(s) -
Liu Xiaodong,
Nordin John H.
Publication year - 1998
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1998)38:3<109::aid-arch1>3.0.co;2-n
Subject(s) - yolk , biology , antiserum , polyclonal antibodies , vitellogenesis , immunogen , affinity chromatography , embryo , protease , antibody , vitellogenin , biochemistry , microbiology and biotechnology , enzyme , oocyte , immunology , monoclonal antibody , ecology , gene
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. Arch. Insect Biochem. Physiol. 38:109–118, 1998. © 1998 Wiley‐Liss, Inc.