Open AccessAntigenic separation of a nonkinin-generating TAMe esterase from human urinary kallikrein and immunohistochemical comparison of their localization in the kidney.
Author(s) -
Geraldine S. Pinkus,
Onesmo K. ole-MoiYoi,
K. Frank Austen,
J Spragg
Publication year - 1981
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 - 10.1177/29.1.7009729
Subject(s) - immunoperoxidase , distal convoluted tubule , tubule , antiserum , convoluted tubule , macula densa , nephron , kallikrein , loop of henle , immunohistochemistry , kidney , chemistry , esterase , microbiology and biotechnology , reabsorption , antigen , biology , enzyme , biochemistry , endocrinology , renin–angiotensin system , antibody , immunology , monoclonal antibody , blood pressure
Two urinary enzymes that cleave alpha-N-p-tosyl-L-arginine methyl ester (TAMe) have been separated and utilized to elicit monospecific antisera; only one, urinary kallikrein (urokallikrein), had kinin-generating activity. The nonkinin-generating TAMe esterase and urokallikrein were antigenically unrelated. Immunoperoxidase studies of normal human kidney revealed localization of nonkinin-generating TAMe esterase to epithelial cells of the distal tubule, including the ascending thick limb, the macula densa region, and some areas of convoluted tubule. Immunoreactivity for urokallikrein was confined to reabsorption droplets of proximal tubules and to focal segments of the distal convoluted tubules. Electrophoretic, antigenic, and immunohistochemical studies have established that urokallikrein and a nonkinin-generating TAMe esterase represent two distinct renal distal tubule enzymes.
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