Repository logo
  • English
  • Čeština
  • Deutsch
  • Español
  • Français
  • Gàidhlig
  • Latviešu
  • Magyar
  • Nederlands
  • Português
  • Português do Brasil
  • Suomi
  • Svenska
  • Türkçe
  • Қазақ
  • বাংলা
  • हिंदी
  • Ελληνικά
  • Log In
    or
    New user? Click here to register.
Repository logo

Repositorio Institucional de la Universidad de Murcia

Repository logoRepository logo
  • Communities & Collections
  • All of DSpace
  • Statistics
  • menu.section.collectors
  • menu.section.acerca
  • English
  • Čeština
  • Deutsch
  • Español
  • Français
  • Gàidhlig
  • Latviešu
  • Magyar
  • Nederlands
  • Português
  • Português do Brasil
  • Suomi
  • Svenska
  • Türkçe
  • Қазақ
  • বাংলা
  • हिंदी
  • Ελληνικά
  • Log In
    or
    New user? Click here to register.
  1. Home
  2. Browse by Subject

Browsing by Subject "Trimetaphosphatase"

Now showing 1 - 1 of 1
Results Per Page
Sort Options
  • Loading...
    Thumbnail Image
    Publication
    Open Access
    Ultracytochemical study of trimetaphosphatase activity during acrosomal formation in the mouse testis
    (Murcia : F. Hernández, 1995) Jin, Q.S.; Kamata, M.; García del Saz, E.; Seguchi, H.
    The localization of Trimetaphosphatase (TMPase) activity during the acrosomal formation in the mouse testis was enzyme cytochemically investigated by the cerium-salt method. In addition to the lysosomes of the Sertoli cells and the spermatogenic cells in the seminiferous tubules, positive TMPase activity was detected in the Golgi complex and in the acrosomal vesicles of the spermatids, as well as in the acrosomes of both spermatids and spermatozoa. In the Golgi complex of the spermatids, TMPase activity was observed in the first one or two lamellae of the trans-face and in the small vesicles in the vicinity of the Golgi complex. TMPase positive reaction was also detected in the acrosomes of the spermatozoa in the lumina of both the seminiferous tubules and the epididymal duct. The localization of this enzyme activity was compared with that of acid phosphatase (ACPase), as detected by the cerium-based method, using B-glycerophosphate as substrate: ACPase activity was completely absent from the Golgi complex, small vesicles, acrosomal vesicle and acrosome throughout the entire process of acrosomal formation. TMPase is thought to become one of the acrosomal components, and may be involved in the acrosomal reaction during fertilization. .

DSpace software copyright © 2002-2026 LYRASIS

  • Cookie settings
  • Accessibility
  • Send Feedback