A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.
Open Access
- 1 March 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (5), 1971-1977
- https://doi.org/10.1016/s0021-9258(19)85978-1
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
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- Subunit interactions in aspartate transcarbamylase. The interaction between catalytic and regulatory subunits and the effect of ligandsJournal of Biological Chemistry, 1975
- Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide ChainsProceedings of the National Academy of Sciences, 1974
- Pathways of Assembly of Aspartate Transcarbamoylase from Catalytic and Regulatory SubunitsProceedings of the National Academy of Sciences, 1974
- Aspartate Transcarbamoylase Molecules Lacking One Regulatory SubunitProceedings of the National Academy of Sciences, 1974
- Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylaseBiochemistry, 1973
- Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analogBiochemistry, 1973
- The Enzymology of Control by Feedback InhibitionJournal of Biological Chemistry, 1962