Immunocytochemical localization of hepatic legandin and Z protein utilizing frozen sections for light and electron microscopy.
Author(s) -
F. Capron,
B Coltoff-Schiller,
Toby Johnson,
G Fleischner,
Sidney Goldfischer
Publication year - 1979
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/27.5.479557
Subject(s) - endoplasmic reticulum , electron microscope , immunocytochemistry , cytosol , chemistry , biophysics , subcellular localization , cytoplasm , biochemistry , biology , enzyme , physics , optics , endocrinology
Ligandin (glutathione-s-transferase) and Z protein are soluble hepatocellular proteins that are involved in the transfer of organic ions, including bilirubin and some hormones and carcinogens from the plasma to the liver. The intracellular distribution of ligandin and Z protein was studied by applying the peroxidase-antiperoxidase procedure of L. A. Sternberger (Immunocytochemistry, Prentice Hall Inc., 1974) to paraffin sections and free-floating 10-micrometers frozen sections that were processed for both light and electron microscopy. Ligandin and Z protein were localized to the cytosol of hepatocytes in association with smooth endoplasmic reticulum (SER), but no reaction product was present between cisternae of rough endoplasmic reticulum. Penetration of reagents was enhanced in 10-micrometers frozen sections and the preservation of subcellular structures was equivalent to thicker, unfrozen sections.
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