Dissection of the active site of rabbit liver tRNA nucleotidyltransferase. Specificity and properties of subsites for donor nucleotide triphosphates.
Open Access
- 1 December 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (23) , 11240-11246
- https://doi.org/10.1016/s0021-9258(19)70281-6
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Dissection of the active site of rabbit liver tRNA nucleotidyltransferase. Specificity and properties of the tRNA and acceptor subsites determined with model acceptor substrates.Journal of Biological Chemistry, 1980
- Separation of functionally distinct regions of a macromolecular substrate. Stimulation of tRNA nucleotidyltransferase by a nonreacting fragment of tRNA.Journal of Biological Chemistry, 1979
- Kinetic analysis of rabbit liver tRNA nucleotidyltransferase.Journal of Biological Chemistry, 1978
- The dinucleoside monophosphate, CpC, is a model acceptor substrate for rabbit‐liver tRNA nucleotidyltransferaseFEBS Letters, 1977
- Pyruvate Carboxylase Affinity Labelling of the Magnesium Adenosine Triphosphate Binding SiteEuropean Journal of Biochemistry, 1976
- Studies on tRNA Nucleotidyltransferase from Baker's YeastEuropean Journal of Biochemistry, 1974
- Reactions at the 3′ Terminus of Transfer Ribonucleic AcidPublished by Elsevier ,1973
- Reactions at the 3′ Terminus of Transfer Ribonucleic AcidPublished by Elsevier ,1973
- Synthesis and Functions of the -C-C-A Terminus of Transfer RNAProgress in Nucleic Acid Research and Molecular Biology, 1973
- Reactions at the 3′ Terminus of Transfer Ribonucleic AcidPublished by Elsevier ,1972