ACTA HISTOCHEMICA ET CYTOCHEMICA
Online ISSN : 1347-5800
Print ISSN : 0044-5991
ISSN-L : 0044-5991
Volume 4, Issue 4
Displaying 1-6 of 6 articles from this issue
  • YASUMASA ISHIBASHI, MICHIHITO NIIMURA, TARO KAWAMURA
    1971 Volume 4 Issue 4 Pages 191-198
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
    Cholinesterase activity (ChA) in human Haarscheiben was ultrastructurally examined with Karnovsky's method and following results were obtained: 1) No ChA was observed on the membrane of myelinated nerve fibers. 2) Axons of non-myelinated nerves in the corium showed strikingly positive ChA on its membrane. 3) The membrane of Tastmeniscus revealed sometimes also positive ChA, but the part of it attached to Merkel cells in the epidermis showed frequently no ChA. 4) On the membrane of the prickle-like cytoplasmic protrusions of the Merkel cell positive, but not so typical ChA was also observed.
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  • TAKASHI IWAYAMA
    1971 Volume 4 Issue 4 Pages 199-207
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
    Phosphatase activities are observed in the gustatory epithelium of rats and rabbits. Among nucleoside phosphatases, ATPase activity is present on taste hairs, the membrane of taste bud cells, subgemmal nerve fibers and capillary walls. The ATPase activity on the membrane of taste bud cells can be differentiated from that of the other sites using PCMB (2.5×10-5M). With an electron microscope, the reaction product is present between intragemmal nerve fibers and dark cells, whereas it is almost absent on the site in contact with the light cell.
    An intense alkaline phosphatase activity is present on the superficial layers of the epithelium covering the gutter of foliate and circumvallate papillae. The activity disappears and reappears according to the decrease and increase of taste buds after denervation and reinnervation of the glosso-pharyngeal nerve. Alk. Pase is not localized on the fungiform papilla in control, but is clearly demonstrated after fasting and the suppression of salivation. The results suggest that alk. Pase may be secreted from the taste bud of fungiform papillae as well as from those of circumvallate and foliate papillae.
    The taste bud shows an intense activity for acid Pase. The reaction product is localized in the supranuclear region of the cell.
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  • TETSUO ISHII
    1971 Volume 4 Issue 4 Pages 208-213
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
    In the human olfactory mucosa, the author demonstrated activities of oxidative enzymes succinic, lactic, malic dehydrogenases and NADH-diaphorase), lysosomal enzymes (acid phosphatase, β-glucuronidase, N-acetyl-β-glucosaminidase), alanyl- and leucyl-aminopeptidases, adenosine triphosphatase (ATPase) and cholinesterase (ChE), The olfactory and supporting cells and Bowman's gland cells showed intense activities of oxidative and lysosomal enzymes. The activity of aminopeptidases was found to be intense in Bowman's gland, while ATPase activity was present in the walls of arteries and veins. ChE activity was restrictedly observed in the nerve fibers around Bowman's gland and arteries, No ChE-active nerves were found in the olfactory epithelia and nerves.
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  • YUTAKA KANEKO
    1971 Volume 4 Issue 4 Pages 214-225
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
    Histochemical investigation of acetylcholinesterase in the organ of Corti has been carried out by means of the Karnovsky's method. Acetylcholinesterase is located on the bottom of outer hair cells, tunnel radial fibers (upper), tunnel spiral bundle and inner spiral bundle. No reacrion was found on the bottom of inner hair cells, lower tunnel radial fibers, outer spiral bundle and bottom of outer hair cells on the outer raw at upper turns. In the bottom of outer hair cells, only vesiculated nerve endings showed the activity of acetylcholinesterase on their plasma membrane. In the basal and middle turns, it is assumed that the reaction products or enzyme from vesiculated nerve endings diffused to non-vesiculated nerve endings.
    On the endolymphatic surface of hair cells, acetylcholinesterase activity was also found but was lower than the activity on the vesiculated nerve endings at the bottom of the hair cells. In addition, some reductive reaction was found on the surface of the hair cells.
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  • SHOZO NISHIDA, MIKIO MIYATA
    1971 Volume 4 Issue 4 Pages 226-241
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
    The albino rat retina was treated by 1% digitonin solution and electron-microscopy was performed. ATPase activity in the outer segment did not appeared to be influenced by the digitonin treatment.
    Electrophoresis indicated that the outer segment lees kept a conspicuous ATPase activity but rhodopsin band was free from ATPase activity.
    Biochemical assay demonstrated that ATPase activity in the outer segment highly depended on Na and K ions.
    The homogenate of the frog retina showed a high dehydrogenase activity to retinol as a substrate, but a very low activity to ethanol.
    ADH activity was histochemically detected in the outer segment on an albino rat retina and optimal pH of phosphate buffer for the tissue reaction seemed to be between 7.8-8.0 than 7.4.
    Electronmicroscopically formazan deposit was detected on the electron dense layer of the outer segment lamellae. Formazan deposit of ten arranged to surround a disc of about 50Å in diameter on the electron dense layer.
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  • 1971 Volume 4 Issue 4 Pages 242-281
    Published: 1971
    Released on J-STAGE: October 28, 2009
    JOURNAL FREE ACCESS
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