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- W3036004564 abstract "During the past three decades, the freeze substitution fixation technique has been developed to observe fine morphology in close to the living state. Recently, this freeze substitution fixation has been successfully applied to enzyme histochemistry demonstrating the active sites of enzymes as well as their active state at the time of quenching. in this study, we have undertaken to study guanosine triphosphatase (GTPase), one of the key enzymes in the cGMP cascade, on the rod outer segment after freeze substitution fixation and have compared the results with those obtained from conventional immersion fixation enzyme histochemistry at the ultrastructural level. Freeze substitution fixation: After Nembutal anesthesia, frog, Xenopus laevis , eyes were excised and the neural retinae were gently separated from the pigment epithelium. The retinae were then rapid frozen using a quick freezing device, the E7200 Slammer (Polaron, Equipment Ltd. England), contacting on an ultrapure copper block at -196°C of liquid nitrogen." @default.
- W3036004564 created "2020-06-25" @default.
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- W3036004564 date "1990-08-12" @default.
- W3036004564 modified "2023-09-25" @default.
- W3036004564 title "Guanosine triphosphatase activity demonstrated by freeze substitution enzyme histochemistry" @default.
- W3036004564 cites W2317195770 @default.
- W3036004564 doi "https://doi.org/10.1017/s0424820100161990" @default.
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