用光镜和电子显微镜联合观察大鼠肝脏无固定冷冻切片中5′-核苷酸酶的活性。

The Histochemical Journal Pub Date : 1995-11-01
J Song, K S Bosch, W Tigchelaar, R J Van Den Munckhof, J P Schellens, C J Van Noorden, W M Frederiks
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引用次数: 0

摘要

在本研究中,利用半透膜在光镜和电子显微镜水平上开发了一种技术来证明5'-核苷酸酶在大鼠肝脏非固定低温切片中的活性。为了尽可能保留未固定材料的超微结构,孵育也在4℃而不是37℃进行。优化的孵育培养基为300 mM马来酸三酯缓冲液,pH为7.2,5 mM单磷酸腺苷为底物,30 mM氯化铈为游离磷酸盐的捕集剂,10 mM氯化镁为活化剂,1.5%琼脂。光镜下,在37℃和4℃孵育时,获得了类似的5′-核苷酸酶活性定位。酶活性主要存在于肝细胞的胆小管膜和窦膜;中心周围的总活性高于门静脉周围。细胞光度分析显示,在37℃下,最终反应产物(FRP)(试验减去对照反应)的形成随时间呈双曲曲线。在高达8微克的截面厚度和玻璃钢的具体用量之间发现了线性关系。在37℃下孵育30 min后,5′-核苷酸酶活性比在4℃下孵育约高3倍。电镜观察显示,半透膜上附着无固定低温切片孵育后,大鼠肝脏超微结构保存较好,肝细胞胆小管和窦质膜上可见电子致密FRP。与4℃孵育相比,37℃孵育后超微结构最明显的变化是在37℃时胆小管处出现多层结构。我们得出结论,本方法在光镜和电镜水平上都有效地证明了大鼠肝脏未固定低温切片中5'-核苷酸酶的活性,并且低温孵育大大改善了超微结构形态。
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Demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver using a combined light- and electron-microscope procedure.

In the present study a technique was developed to demonstrate 5'-nucleotidase activity in unfixed cryostat sections of rat liver at the light- and electron-microscope level using a semipermeable membrane. In order to retain the ultrastructure of the unfixed material as much as possible, incubations were also performed at 4 degrees C rather than at 37 degrees C. The optimized incubation medium contained 300 mM Tris-maleate buffer, pH 7.2, 5 mM adenosine monophosphate as substrate, 30 mM cerium chloride as capturing agent for liberated phosphate, 10 mM magnesium chloride as activator and 1.5% agar. At the light-microscope level, similar localizations of 5'-nucleotidase activity were obtained when incubations were performed at 37 degrees C and 4 degrees C. Enzyme activity was present mainly at bile canalicular membranes and at sinusoidal membranes of hepatocytes; total activity was higher in pericentral than in periportal areas. Cytophotometric analyses revealed that specific formation of final reaction product (FRP) (test minus control reaction) at 37 degrees C followed a hyperbolic curve with time. A linear relationship was found between specific amounts of FRP and section thickness up to 8 micrograms. 5'-Nucleotidase activity was about three-fold higher after incubation for 30 min at 37 degrees C than at 4 degrees C. At the electron-microscope level, it was demonstrated that the ultrastructure of rat liver was rather well-preserved after incubating unfixed cryostat sections attached to a semipermeable membrane and electron-dense FRP was found at bile canalicular and sinusoidal plasma membrane of hepatocytes. The most distinct changes in ultrastructure after incubation at 37 degrees C, in comparison with that at 4 degrees C, were the appearance of multi-lamellar structures at bile canaliculi at 37 degrees C. We conclude that the present method is valid for the demonstration of 5'-nucleotidase activity in unfixed cryostat sections of rat liver at both the light- and electron-microscope levels and that hypothermic incubations improve ultrastructural morphology substantially.

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