The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Dihydrofolate reductase: thymidylate synthase, a bifunctional polypeptide from Crithidia fasciculata.
Abstract
The molecular weight of dihydrofolate reductase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) from protozoa has been reported to be 5- to 10-fold larger than the isofunctional enzyme of most other organisms studied, based on gel filtration. This enzyme from the protozoal flagellate Crithidia fasciculata has been purified to homogeneity and found to be a bifunctional protein with thymidylate synthase (5,10-methylene tetrahydrofolate:dUMP C-methyltransferase, EC 2.1.1.45) activity. The purified protein, eluted from methotrexate-Sepharose columns by dihydrofolate, migrated as a single band on both nondenaturing and denaturing polyacrylamide gel electrophoresis. The monomer Mr is 56,700 +/- 200. The native Mr was calculated to be 107,000 from a sedimentation coefficient of 5.9 and Stokes radius of 4.4 nm. Dihydrofolate reductase and thymidylate synthase activities of the rodent malaria organism Plasmodium berghei also copurified on Sephadex G-200 and methotexate-Sepharose columns, suggesting that this unique bifunctional protein might occur throughout the Protozoa.
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“Detection of genuine gene fusion events has been reported long before the first complete genomes became available (110,111), but beyond that point they have been proven instrumental in detecting gene/protein associations with high specificity (112,113).”
From Tandem repeats lead to sequence assembly errors and impose multi-level challenges for genome and protein databases (2019) · cites this paper as [111]
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Enzyme Inhibition in Relation to Chemotherapy.
Ackermann, W. W., & Potter, V. R. (1949) · Experimental Biology and Medicine · doi:10.3181/00379727-72-17313 · Cited by 262
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Metadata
- Authors
- Ferone, R., & Roland, S.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1980-10
- Volume
- 77
- Issue
- 10
- Pages
- 5802-5806
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 85
- References
- 1
- Language
- en
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