1985
DOI: 10.2330/joralbiosci1965.27.702
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Immunohistochemical demonstration of amylase in normal and neoplastic salivary glands.

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Cited by 5 publications
(2 citation statements)
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“…Numerous studies have been carried out to localize the various proteins in different salivary glands (Tourville et al, 1969;Kraus and Mestecky, 1971;Klockars and Reitamo, 1975;Mason and Taylor, 1975;Reitamo et al, 1980;Korsrud and Brandtzaeg, 1982). a-Amylase comprises the major protein component of parotid gland, and there is substantial histochemical evidence to show that the enzyme is produced and secreted by the serous acinar cells (Vreugdenhil et al, 1982;Hatakeyama et al, 1985).…”
mentioning
confidence: 99%
“…Numerous studies have been carried out to localize the various proteins in different salivary glands (Tourville et al, 1969;Kraus and Mestecky, 1971;Klockars and Reitamo, 1975;Mason and Taylor, 1975;Reitamo et al, 1980;Korsrud and Brandtzaeg, 1982). a-Amylase comprises the major protein component of parotid gland, and there is substantial histochemical evidence to show that the enzyme is produced and secreted by the serous acinar cells (Vreugdenhil et al, 1982;Hatakeyama et al, 1985).…”
mentioning
confidence: 99%
“…The Immunohistochemistry (IHC) staining for the alpha‐smooth‐muscle actin (alpha SMA) and salivary alpha‐amylase was done using the standard protocol to detect myoepithelial cells and salivary amylase in the walls of the seromucous acini of the examined tissues. Owing to the known presence of the myoepithelial cells (Balachander et al, 2015) and salivary amylase in the acini of the salivary glands (Hatakeyama et al, 1985), the submandibular gland was used as a positive control. The 5μ thick paraffin‐embedded tissue sections were mounted on the frosted slides coated with Poly‐ l ‐Lysine solution.…”
Section: Methodsmentioning
confidence: 99%