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ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein
Selective extraction of specific cell components by enzyme or acid hydrolysis is possible from ultrathin sections for electron microscopy and parallel 2 µ sections for light microscopy of tissues fixed in formalin and embedded in a water-soluble polyepoxide, product X133/2097. Normal rat tissues fix...
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1961
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225089/ https://www.ncbi.nlm.nih.gov/pubmed/13760208 |
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author | Leduc, Elizabeth H. Bernhard, Wilhelm |
author_facet | Leduc, Elizabeth H. Bernhard, Wilhelm |
author_sort | Leduc, Elizabeth H. |
collection | PubMed |
description | Selective extraction of specific cell components by enzyme or acid hydrolysis is possible from ultrathin sections for electron microscopy and parallel 2 µ sections for light microscopy of tissues fixed in formalin and embedded in a water-soluble polyepoxide, product X133/2097. Normal rat tissues fixed 15 minutes in formalin at 3°C are more rapidly digested by proteinases than those fixed for the same length of time at 20°C. Trypsin selectively attacks the nuclear chromatin and the ribonucleoprotein particles of the ergastroplasm, whereas mitochondria and zymogen granules resist tryptic digestion. Pepsin rapidly attacks the mitochondria and zymogen granules. The ergastoplasm and nucleus at first resist peptic digestion, but in time the entire cytoplasm and interchromatinic portion of the nucleus are attacked. Ribonuclease abolishes cytoplasmic basophilia in 2 µ sections, but parallel ultra-thin sections, stained with uranyl acetate and examined in the electron microscope, show no change in the ribonucleoprotein particles of the ergastoplasm. Desoxyribonuclease alone had no effect, but after pretreatment of the sections with pepsin or hydrochloric acid, desoxyribonuclease specifically attacked the nuclear chromatin. Nucleic acid-containing structures in the sections are gradually disintegrated by perchloric acid or hydrochloric acid. |
format | Text |
id | pubmed-2225089 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1961 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22250892008-05-01 ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein Leduc, Elizabeth H. Bernhard, Wilhelm J Biophys Biochem Cytol Article Selective extraction of specific cell components by enzyme or acid hydrolysis is possible from ultrathin sections for electron microscopy and parallel 2 µ sections for light microscopy of tissues fixed in formalin and embedded in a water-soluble polyepoxide, product X133/2097. Normal rat tissues fixed 15 minutes in formalin at 3°C are more rapidly digested by proteinases than those fixed for the same length of time at 20°C. Trypsin selectively attacks the nuclear chromatin and the ribonucleoprotein particles of the ergastroplasm, whereas mitochondria and zymogen granules resist tryptic digestion. Pepsin rapidly attacks the mitochondria and zymogen granules. The ergastoplasm and nucleus at first resist peptic digestion, but in time the entire cytoplasm and interchromatinic portion of the nucleus are attacked. Ribonuclease abolishes cytoplasmic basophilia in 2 µ sections, but parallel ultra-thin sections, stained with uranyl acetate and examined in the electron microscope, show no change in the ribonucleoprotein particles of the ergastoplasm. Desoxyribonuclease alone had no effect, but after pretreatment of the sections with pepsin or hydrochloric acid, desoxyribonuclease specifically attacked the nuclear chromatin. Nucleic acid-containing structures in the sections are gradually disintegrated by perchloric acid or hydrochloric acid. The Rockefeller University Press 1961-07-01 /pmc/articles/PMC2225089/ /pubmed/13760208 Text en Copyright © Copyright, 1961, by The Rockefeller Institute Press |
spellingShingle | Article Leduc, Elizabeth H. Bernhard, Wilhelm ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title | ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title_full | ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title_fullStr | ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title_full_unstemmed | ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title_short | ULTRASTRUCTURAL CYTOCHEMISTRY : Enzyme and Acid Hydrolysis of Nucleic Acids and Protein |
title_sort | ultrastructural cytochemistry : enzyme and acid hydrolysis of nucleic acids and protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225089/ https://www.ncbi.nlm.nih.gov/pubmed/13760208 |
work_keys_str_mv | AT leducelizabethh ultrastructuralcytochemistryenzymeandacidhydrolysisofnucleicacidsandprotein AT bernhardwilhelm ultrastructuralcytochemistryenzymeandacidhydrolysisofnucleicacidsandprotein |