[Alkaline phosphatase properties of the olfactory lining of the bull].
Biochemical and electrophoretic characteristics of enzyme alkaline phosphatase and its localization in the bull's olfactory mucose structures have been investigated. The activity of enzymes was found to change with odour stimulation. Using electron microscope histochemistry a considerable activity of this enzyme has been demonstrated in the structures secreting olfactory mucus, and in the mucus itself, with alkaline phosphatase macromolecules being concentrated on the surface membrane of olfactory cilia, forming a layer around these. The activity of alkaline phosphatase was found in some receptor cells. The electrophoretic analysis allowed to find five molecular forms of alkaline phosphatase, having different substrate specificity. Isoenzymes II and III, splitting alpha-sodium naphthylphosphate, displayed similar properties with those of intestinal serum isoenzymes. Other three of the five isoenzymes of olfactorymucose have no analogues in the serum that could be regarded as a possible involvement in olfactory epithelium of phosphatases performing specific functions typical of this receptor organ.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004848:Epithelium / Q000648:ultrastructure; D006651:Histocytochemistry; D008297:Male; D008854:Microscopy, Electron; D009831:Olfactory Mucosa / Q000201:enzymology* / Q000648:ultrastructure
D000469:Alkaline Phosphatase
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