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Some characteristic reactions catalysed by the ribonuclease activity in sections from fixed tissues

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Zeitschrift für Zellforschung und mikroskopische Anatomie Abt. Histochemie Aims and scope Submit manuscript

Summary

1. The ribonuclease activity in sections from freeze-dried Carnoy-fixed rat pancreas has been characterized through studies on the products of interaction with synthetic nucleoside derivatives, nucleotide esters, and of the polynucleotide synthetic properties.

2. Homogenates of the sections in McIlvaine's buffer atph 7.0 degrade pyrimidine 2′:3′-phosphates to the corresponding 3′-dihydrogen phosphate, and the purine derivatives at a much slower rate.

3. Synthetic cytidylyl-cytidine, and benzyl- and ethyl-3′-esters of pyrimidine nucleotides are degraded to nucleoside 3′-phosphates. All the purine, and the 2′-esters of pyrimidine nucleotides are not affected during 24 hours of incubation.

4. Under influence of the homogenates, ribopolynucleotides will readily be synthesized from cytidine-2′:3′-phosphate and cytidine, the 3′-P-5′dinucleotide links being identified in cytidylyl-cytidine and cyclic dicytidylic acid.

5. The conclusion is reached that the activity of the sections coincides with the DEase and CPase activity of crystalline pancreatic RNase. Some aspects of the possibilities for the histochemical localization of the activity are briefly discussed.

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Aided by grants from the Royal Physiographic Society of Lund, the Nora Sörensson Foundation, and the J. V. and Charlotta Lundgren Foundation.

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Ehinger, B., Lagerstedt, S. Some characteristic reactions catalysed by the ribonuclease activity in sections from fixed tissues. Histochemie 1, 331–342 (1959). https://doi.org/10.1007/BF00737705

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