Document Detail


Effect of nucleic-acid-binding compounds on the hydrolytic activity of various ribonucleases.
MedLine Citation:
PMID:  1204647     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Studies were conducted on the stimulatory effect that various nucleic-acid-binding compounds have on the hydrolysis of RNA and polyribonucleotides by pancreatic ribonuclease A and by other ribonucleases. The stimulatory activity of chloroquine on tRNA hydrolysis by pancreatic ribonuclease was due to the formation of oligonucleotides of a wide range of sizes and was not due to the formation of very short ( n greater than 5) oligonucleotide fragments of tRNA. The dextrorotatory and levorotatory isomers of chloroquine did not differ in their ability to stimulate the hydrolysis of tRNA by pancreatic ribonuclease A. In addition to chloroquine and primaquine, other nucleic-acid-binding compounds (e.g., quinacrine, lucanthone, and proflavin) stimulated the hydrolysis of tRNA by pancreatic ribonuclease A. Chloroquine did not alter the rate of hydrolysis by pancreatic ribonuclease A of low-molecular-weight substrates (cytidine cyclic 2':o'-monophosphate, uridine cyclic 2':3'-monophosphate, cytidylyl-adenosine, or uridylyl-uridine). Furthermore, chloroquine and primaquine did not affect the hydrolysis of poly(A) by high concentrations of pancreatic ribonuclease A. In studies on the hydrolysis of tRNA by other endoribonucleases, several of the nucleic-acid-binding compounds (e.g., quinacrine and ethidium) exhibited appreciable inhibition of both ribonuclease N1 and ribonuclease T1. None of the compounds tested stimulated the activity of ribonuclease T1, and only chloroquine, and perhaps lucanthone, stimulated the hydrolysis of tRNA by ribonuclease N1.
Authors:
D J Holbrook; L P Wichard; M E Washington
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  60     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1975 Dec 
Date Detail:
Created Date:  1976-03-30     Completed Date:  1976-03-30     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:  317-24     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acridines / pharmacology*
Aminoquinolines / pharmacology*
Animals
Binding Sites
Cattle
Chloroquine / pharmacology*
Ethidium / pharmacology
Kinetics
Pancreas / enzymology
Primaquine / pharmacology*
Proflavine / pharmacology*
Protein Binding
Quinacrine / pharmacology*
Ribonucleases / metabolism*
Spermidine / pharmacology
Spermine / pharmacology
Structure-Activity Relationship
Chemical
Reg. No./Substance:
0/Acridines; 0/Aminoquinolines; 124-20-9/Spermidine; 3546-21-2/Ethidium; 54-05-7/Chloroquine; 71-44-3/Spermine; 83-89-6/Quinacrine; 90-34-6/Primaquine; 92-62-6/Proflavine; EC 3.1.-/Ribonucleases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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