Skip Navigation

This Article
Right arrow Print PDF (527K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Darling, T. L.
Right arrow Articles by Reid, T. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Darling, T. L.
Right arrow Articles by Reid, T. W.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1979, Vol. 6, No. 3 1189-1201
© 1979


Articles

Apparent allosterism by avian myeloblastosis virus reverse transcriptase and E coli DNA polymerase I

Thomas L. Darling* and Ted W. Reid+

*Department of Neurobiology, Stanford University Stanford, CA 94305 USA +Department of Ophthalmology and Visual Science, Yale University School of Medicine New Haven, CT 06510, USA

Received November 1, 1978. A recent report (1) presented evidence for allosterism in reverse transcription by Mason-Pfizer monkey virus reverse transcriptase and by E. coli DNA polymerase I. Our experiments also demonstrate these apparent cooperative effects when synthesis is catalyzed by either avian myeloblastosis virus DNA polymerase, feline sarcoma virus DNA polymerase, or E. coli DNA polymerase I (large fragment). We show that the apparent cooperativity depends on the use of oligo(dT)12– as primer. However, if the polymerase reaction products are isolated chromatographically, then the polymerases obey classical Michaelis Menten kinetics with respect to substrate and enzyme concentrations. These results suggest that the cooperative effects are an acid precipitation artifact. The results are also consistent with the enzyme operating by a distributive mechanism with the oligo(dT)12–18 primer.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.