Adenosine triphosphate-adenosine-5'-monophosphate phosphotransferase from normal human liver mitochondria. Isolation, chemical properties, and immunochemical comparison with Duchenne dystrophic serum aberrant adenylate kinase.
Open Access
- 1 November 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (21) , 13120-13128
- https://doi.org/10.1016/s0021-9258(18)33631-7
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- An aberrant adenylate kinase isoenzyme from the serum of patients with Duchenne muscular dystrophyBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Purification and characterization of adenylate kinase isozymes from rat muscle and liverBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Purification and Characterization of Acidic Adenylate Kinase in Porcine HeartEuropean Journal of Biochemistry, 1978
- The Amino‐Acid Sequence of Porcine Adenylate Kinase from Skeletal MuscleEuropean Journal of Biochemistry, 1974
- Column chromatography of amino acids with fluorescence detectionJournal of Chromatography A, 1973
- Purification of rat liver adenylate kinase isozyme II and comparison with isozyme IIIBiochimica et Biophysica Acta (BBA) - Enzymology, 1972
- Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridineArchives of Biochemistry and Biophysics, 1967
- Graphical determination of the dissociation constants for two-substrate enzyme systemsBiochimica et Biophysica Acta, 1957
- Initial Steady State Velocities in the Evaluation of Enzyme-Coenzyme-Substrate Reaction Mechanisms.Acta Chemica Scandinavica, 1957
- Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic MercurialsJournal of the American Chemical Society, 1954