Inhibition of avian myeloblastosis virus reverse transcriptase and virus inactivation by metal complexes of isonicotinic acid hydrazide
Data(s) |
01/10/1982
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Resumo |
The cupric and ferric complexes of isonicotinic acid hydrazide (INH) inhibit the DNA synthesis catalysed by avian myeloblastosis virus (AMV) reverse transcriptase. The inhibition was to the extent of 95% by 50 μM of cupric-INH complex and 55% by 100 μM of ferric-INH complex. These complexes have been found to bind preferentially to the enzyme than to the template-primer. Kinetic analysis showed that the cupric-INH complex is a non-competitive inhibitor with respect to dTTP. The time course of inhibition has revealed that the complexes are inhibitory even after the initiation of polynucleotide synthesis. In vivo toxicity studies in 1-day-old chicks have shown that the complexes are not toxic up to a concentration of 500 μg per chick. Infection of the 1-day-old chicks with AMV pretreated with 150 μg of either of the complexes prevented symptoms of leukemia due to virus inactivation. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/20306/1/fulltext.pdf Vasudevachari, MB and Antony, A (1982) Inhibition of avian myeloblastosis virus reverse transcriptase and virus inactivation by metal complexes of isonicotinic acid hydrazide. In: Antiviral Research, 2 (5). pp. 291-300. |
Publicador |
Elsevier Science |
Relação |
http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T2H-476F415-3V&_user=512776&_rdoc=1&_fmt=&_orig=search&_sort=d&_docanchor=&view=c&_acct=C000025298&_version=1&_urlVersion=0&_userid=512776&md5=c7a283462f004a5ec94edba374d6966b http://eprints.iisc.ernet.in/20306/ |
Palavras-Chave | #Microbiology & Cell Biology |
Tipo |
Journal Article PeerReviewed |