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J. Biochem, 1982, Vol. 91, No. 1 311-322
© 1982 Japanese Biochemical Society

research-article

Reverse Transcriptase Associated with Avian Sarcoma-Leukosis Viruses. I. Comparison of Intra-Virion Content of Multiple Enzyme Forms1

Akemichi UENO*,2, Akira ISHIHAMA**,3 and Kumao TOYOSHIMA*,***

*Research Institute for Microbial Diseases, Osaka University Suita, Osaka 565
**Institute for Virus Research, Kyoto University Sakyo-ku, Kyoto, Kyoto 606
***Institute of Medical Science, The University of Tokyo Minato-ku, Tokyo 108

3 To whom correspondence should be addressed

The RNA-dependent DNA polymerase (the reverse transcriptase) was solubilized from three related strains of avian sarcoma virus (ASV B77, ASV tsLA334, and ASV QV2) as well as avian myeloblastosis virus (AMV) and a chicken endogenous virus (RAV-0), by a combination of non-ionic detergent treatment and CsCl step-gradient centrifugation, and was subsequently separated into individual enzyme forms by poly(C)-agarose column chromatography. The newly developed two-step method allowed us to purify the three molecular forms ({alpha}-, {alpha}ß-, and ß-form) of highly active enzyme rapidly and quantitatively from all the five virus strains examined. The molar ratio of the three enzyme forms differed among the virus strains: For the three sarcoma viruses, the major species was the {alpha}ß enzyme, the putative holoenzyme, and the {alpha}- and ß-form enzymes were less than a few percent and 15–25 %, respectively, while the {alpha}-form enzyme content was higher for the two leukosis viruses than for the three sarcoma viruses. Both the total DNA polymerase activity and the content of the two enzyme subunits in purified virions of the three sarcoma virus was in the following order: ASV tsLA334>ASV B77>ASV QV2, which paralleled the virus yield at a permissive temperature in roller bottle cultures of chick embryo fibroblasts. No alteration was found in the thermolability of DNA polymerases between tsLA334, which carries ts mutations affecting both virus growth and cell-transformation, and other viruses.

1 This study was supported in part by grants from the Ministry of Education, Science and Culture of Japan.

2 Present address: Department of Biochemistry, School of Dentistry, Tokushima University, Tokushima, Tokushima 770.


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