Document Detail


A guanyloribonuclease of mouse liver cytosol.
MedLine Citation:
PMID:  2119304     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
A Pantazaki; J G Georgatsos
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  192     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1990 Aug 
Date Detail:
Created Date:  1990-10-24     Completed Date:  1990-10-24     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  115-7     Citation Subset:  IM    
Affiliation:
Laboratory of Biochemistry, Faculty of Chemistry, University of Thessaloniki, Greece.
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MeSH Terms
Descriptor/Qualifier:
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:
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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