Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus

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Standard

Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus. / Jensen, Kaj Frank.

I: Journal of Virology, Bind 28, Nr. 2, 1978, s. 427-433.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Jensen, KF 1978, 'Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus', Journal of Virology, bind 28, nr. 2, s. 427-433. <http://www.ncbi.nlm.nih.gov/pmc/articles/PMC354291/pdf/jvirol00203-0013.pdf>

APA

Jensen, K. F. (1978). Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus. Journal of Virology, 28(2), 427-433. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC354291/pdf/jvirol00203-0013.pdf

Vancouver

Jensen KF. Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus. Journal of Virology. 1978;28(2):427-433.

Author

Jensen, Kaj Frank. / Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus. I: Journal of Virology. 1978 ; Bind 28, Nr. 2. s. 427-433.

Bibtex

@article{8396bc50847b11dcbee902004c4f4f50,
title = "Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus",
abstract = "Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.",
author = "Jensen, {Kaj Frank}",
year = "1978",
language = "English",
volume = "28",
pages = "427--433",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "2",

}

RIS

TY - JOUR

T1 - Detergent inhibited, heat labile nucleoside triphosphatase in cores of avian myeloblastosis virus

AU - Jensen, Kaj Frank

PY - 1978

Y1 - 1978

N2 - Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.

AB - Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.

M3 - Journal article

VL - 28

SP - 427

EP - 433

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 2

ER -

ID: 1393009