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Immunohistochemical study of phospholipase A 2 in boyine prostate
Author(s) -
Rönkkö Seppo
Publication year - 1993
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990220309
Subject(s) - endoplasmic reticulum , polyclonal antibodies , immunogold labelling , prostate , western blot , microbiology and biotechnology , biology , antiserum , phospholipase a2 , immunocytochemistry , immunohistochemistry , chemistry , antibody , enzyme , biochemistry , endocrinology , immunology , genetics , cancer , gene
Approximately 1,100‐fold purified phospholipase A 2 (PLA 2 ) from bovine prostate was injected into rabbit to prepare polyclonal antibodies. Antibodies produced showed specific immunoprecipitation only with the purified enzyme, as well as with homogenate of bovine prostatic tissue. By Western blot analysis or by immunodiffusion test, no cross‐reactivity with PLA 2 purified from human seminal plasma, bovine pancreas, Crotalus adamanteus venom, or with partially purified PLA 2 from bovine seminal vesicle fluid or Cowper's glands was observed. Using the indirect peroxidase technique, PLA 2 was localized in the cytoplasm of bovine prostatic epithelial cells. By immunogold microscopy, this enzyme was directly visualized inside the lysosomes, as well as in the endoplasmic reticulum of the glandular epithelial cells. Enzyme activity was localized in two principal subcellular sites: the mitochondria and lysosome‐enriched fraction, and in the microsomal fraction. © 1993 Wiley‐Liss, Inc.