title: Studies on experimental chlamydial mastitis in goat histoenzymology.
abstract: Two strains of Chlamydia psittaci (one isolated from aborted goat foetus and the other from brain of a buffalo calf that had died of meningoencephalitis) were injected intracisternally into six goats to produce experimental mastitis. Cryostat sections of 7-8 microns thickness, obtained from udder, teat, liver and kidney of infected and control animals were incubated for histoenzymic demonstration of alkaline-(AKPase), acid-(ACPase) and adenosine-tri-(ATPase) phosphatases; lactate-(LDH) and succinate-(SDH) dehydrogenases and for reduced nicotinamide adenine dinucleotide phosphate diaphorase (NADPH-D). Results demonstrated that AKPase and NADPH-D declined while ACPase accumulated in acinar cells of udder while both NADPH-D and ACPase decreased in teat sinus epithelium. Hepatic canaliculi in perilobular areas of liver lobules registered complete absence of AKPase and ATPase. Hepatocytes and renal tubules accumulated LDH, SDH and NADPH-D. The interstitial connective tissue of udder and kidney presented higher levels of AKPase. Comparison of results with biochemical alterations in the level of these enzymes revealed striking discrepancies which seem to arise because of failure of biochemical procedures to discriminate between functional cells of tissue and inflammatory cells. The functional significance of histoenzymic alterations has been discussed.
authors.affiliation: Department of Veterinary Bacteriology and Virology, Punjab Agricultural University, Ludhiana, India.
authors.forename: S
authors.initials: S
authors.lastname: Koul
authors.forename: J
authors.initials: J
authors.lastname: Singh
authors.forename: P N
authors.initials: PN
authors.lastname: Dhingra
authors.forename: G S
authors.initials: GS
authors.lastname: Khatra
mesh_terms: D000818:Animals; D005260:Female; D015511:Goat Diseases / Q000201:enzymology*; D006041:Goats; D007124:Immunoenzyme Techniques / Q000662:veterinary; D007668:Kidney / Q000201:enzymology; D007770:L-Lactate Dehydrogenase / Q000096:biosynthesis; D007774:Lactation / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D008321:Mammary Glands, Animal / Q000201:enzymology; D008413:Mastitis / Q000201:enzymology / Q000662:veterinary*; D009252:NADPH Dehydrogenase / Q000096:biosynthesis; D010088:Oxidoreductases / Q000096:biosynthesis*; D010744:Phosphoric Monoester Hydrolases / Q000096:biosynthesis*; D009956:Psittacosis / Q000201:enzymology / Q000662:veterinary*; D013385:Succinate Dehydrogenase / Q000096:biosynthesis
chemical_list: D010088:Oxidoreductases; D007770:L-Lactate Dehydrogenase; D013385:Succinate Dehydrogenase; D009252:NADPH Dehydrogenase; D010744:Phosphoric Monoester Hydrolases