Open AccessIMMUNOHISTOCHEMICAL LOCALIZATION OF LACTOPEROXIDASE IN BOVINE TISSUES
Author(s) -
Takayuki Harada,
Mitsuo Baba,
Shigeru Morikawa
Publication year - 1973
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 - 10.1177/21.9.804
Subject(s) - lactoperoxidase , serous fluid , immunohistochemistry , chemistry , antibody , pathology , microbiology and biotechnology , antiserum , immunoperoxidase , antigen , biology , biochemistry , peroxidase , enzyme , immunology , medicine , monoclonal antibody
Distribution of lactoperoxidase in bovine tissues was investigated by using fluorescent antibody techniques, and immunochemical properties of the enzyme were also examined. As a result of immunodiffusion, two antigenic components were found, but no cross-reactivity between lactoperoxidase and hemoproteins such as catalase, cytochrome c, hemoglobin or ferritin was observed. Lactoperoxidase was found mainly in the cytoplasm of alveolar cells of the mammary gland; in those acinar cells, which were morphologically identical to serous cells, of the sublingual gland; in acinar cells of the lacrimal gland; and also in some peripheral leukocytes and in a small number of splenic cells in the red pulp. Lactoperoxidase in the alveolar and ductal spaces and in some of the ductal epithelia of those glands was observed after ethanol or acidified ethanol fixation but not after formalin fixation. It has been demonstrated by both the present and previous work (Morikawa and Harada (1969)) that lactoperoxidase and liver-catalase were distinguishable in bovine tissues when fluorescent antibody techniques were utilized.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom