Lack of phosphorylatable site and some kinetic properties of erythrocyte pyruvate kinase from the rat A modified L-type isozyme?
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(78)80626-7/fullpdf
Reference17 articles.
1. Multimolecular Forms of Pyruvate Kinase from Rat and Other Mammalian Tissues*
2. The subunit structure of human muscle and human erythrocyte pyruvate kinase isozymes
3. Human erythrocyte pyruvate kinase Total purification and evidence for its antigenic identity with L-type enzyme
4. Evidence for a postsynthetic proteolytic transformation of human erythrocyte pyruvate kinase into L-type enzyme
5. Two different forms of pyruvate kinase in rat kidney cortex
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1. Purification and regulatory properties of pigeon erythrocyte pyruvate kinase;Comparative Biochemistry and Physiology Part B: Comparative Biochemistry;1989-01
2. 2 Pyruvate Kinase;Control by Phosphorylation Part B - Specific Enzymes (II) Biological Processes;1987
3. Hepatic L-Type Pyruvate Kinase: Separation of Unphosphorylated, Phosphorylated and Proteolytically Modified In Vivo Forms1;The Journal of Biochemistry;1984-04
4. Comparative Studies on Physical Properties Concerned with the Stability of Unphosphorylated, Phosphorylated and Proteolytically Modified L-type Pyruvate Kinase from Pig Liver.;Acta Chemica Scandinavica;1984
5. Studies on the in vitro phosphorylation of 6-phosphofructo-1-kinase from rat liver;Archives of Biochemistry and Biophysics;1982-05
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