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  • 1970-1974  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 21 (1970), S. 170-180 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Uncertainty about the nature of the reduction products of ditetrazolium salts may have limited their use in quantitative histochemistry. Our studies have shown that under appropriate conditions pure Nitro-BT reduces through a red intermediate substance to a stable blue diformazan. Nitrobenzene was found to be a satisfactory solvent for this diformazan. The monotetrazolium INT may also be reduced to a formazan through an intermediate phase. The amounts of definitive formazan produced from both monotetrazolium and ditetrazolium salts may be influenced by the solubility of their intermediate reduction compounds in the systems in which reduction is occurring. The yield of definitive diformazan from Nitro-BT after chemical reduction, and after enzymatic reduction in liver homogenate and sections of a “mock” tissue, was not in linear proportion to the strength of reducing conditions; however, the yields of formazan from the monotetrazoliums INT and MTT were linear. This finding suggests that in quantitative histochemistry it is essential to calibrate reactions involving ditetrazolium reduction.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 27 (1971), S. 21-27 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An investigation has been carried out on the stability of several enzymes in portions of rabbit brain and spinal cord kept at controlled temperatures between 22 and 37° C for periods up to 24 hours before processing for enzyme activity. The enzymes studied were NAD diaphorase, succinate, lactate, glutamate and glucose-6-phosphate dehydrogenases, and monoamine oxidase. One-wavelength “plug” cytophotometric measurements of enzyme activity were carried out on Purkinje cells, neuropil of the granular layer of the cerebellar cortex and on anterior horn cells. Succinate dehydrogenase activity proved to be stable after 24 hours post-mortem exposure at 37°C. Lactate dehydrogenase, NAD diaphorase and monoamine oxidase activities were less stable at the higher temperatures but were stable at 22°C. Glutamate and glucose-6-phosphate dehydrogenase activities fell significantly with exposure at 22°C. It thus appears possible to make valid histochemical measurements of the activities of certain oxidative enzymes in selected post-mortem brain material.
    Type of Medium: Electronic Resource
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