| A guanyloribonuclease of mouse liver cytosol. | |
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MedLine Citation:
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PMID: 2119304 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The acid RNase activity of mouse liver cytosol has been resolved into two different enzymes named acid RNase I and acid RNase II respectively. Acid RNase I is a typical pancreatic-type enzyme hydrolyzing CpN and UpN bonds. Acid RNase II, however, hydrolyzes GpN bonds in non-hydrogen-bonded regions of the substrate. |
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Authors:
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A Pantazaki; J G Georgatsos |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 192 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1990 Aug |
Date Detail:
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Created Date: 1990-10-24 Completed Date: 1990-10-24 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 115-7 Citation Subset: IM |
Affiliation:
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Laboratory of Biochemistry, Faculty of Chemistry, University of Thessaloniki, Greece. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Base Sequence Chromatography, Gel Cytosol / enzymology* Endoribonucleases / metabolism* Exoribonucleases / isolation & purification, metabolism Hydrogen-Ion Concentration Liver / enzymology*, ultrastructure Mice Molecular Sequence Data Ribonuclease T1 / isolation & purification, metabolism* Ribonucleases / metabolism Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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EC 3.1.-/Endoribonucleases; EC 3.1.-/Exoribonucleases; EC 3.1.-/Ribonucleases; EC 3.1.13.1/exoribonuclease II; EC 3.1.27.3/Ribonuclease T1 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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