Cyanate modification of essential lysyl residues of the diphosphopyridine nucleotide-specific isocitrate dehydrogenase of pig heart.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Pig heart triphosphopyridine nucleotide specific isocitrate dehydrogenase. Single polypeptide chain
2. Substrate Independence of Molecular Weight of Triphosphopyridine Nucleotide-specific Isocitrate Dehydrogenase
3. NADP-Linked Isocitrate Dehydrogenase from Beef Liver. Purification, Quaternary Structure and Catalytic Activity
4. DPN-Linked Isocitrate Dehydrogenase of Animal Tissues* *The unpublished experimental work from this laboratory presented here and the preparation of this article have been assisted by a grant from the National Institute of Arthritis and Metabolic Diseases (AM 10501), United States Public Health Service.
5. Effect of Modification of a Methionyl Residue on the Kinetic and Molecular Properties of Isocitrate Dehydrogenase
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1. Cyanate causes depletion of ascorbate in organisms;Biochimica et Biophysica Acta (BBA) - General Subjects;1997-10
2. Carbamylation Decreases the Cytotoxicity but not the Drug-Carrier Properties of Polylysines;Journal of Drug Targeting;1995-01
3. The cyanase operon and cyanate metabolism;FEMS Microbiology Letters;1990-12
4. Carbonic anhydrase inhibition affects contraction of directly stimulated rat soleus;Life Sciences;1988-01
5. Effects of carbamoylating agents on tumor metabolism;Critical Reviews in Oncology/Hematology;1987-01
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