The primary structure of aspartate aminotransferase from pig heart muscle determined in part using a protease with specificity for lysine
- 1 January 1974
- journal article
- Published by Wiley in FEBS Letters
- Vol. 38 (2), 229-233
- https://doi.org/10.1016/0014-5793(74)80120-1
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastaseBiochemical Journal, 1973
- Cytoplasmic Aspartate Aminotransferase: Syncatalytic Sulfhydryl Group ModificationJournal of Biological Chemistry, 1973
- The complete amino acid sequence of cytoplasmic aspartate aminotransferase from pig heartFEBS Letters, 1973
- The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsinBiochemical Journal, 1972
- The position of an essential tyrosine residue in the polypeptide chain of aspartate transaminaseFEBS Letters, 1972
- Cytoplasmic aspartate aminotransferase from pig heart muscle: Partial sequenceFEBS Letters, 1971
- Strategy and tactics in protein chemistryBiochemical Journal, 1970
- Primary structure of pyridoxal phosphate binding site in the mitochondrial and extramitochondrial aspartate aminotransferases from pig heart muscle. Chymotryptic peptidesBiochemistry, 1969
- The Molecular Weight and other Properties of Aspartate Aminotransferase from Pig Heart MuscleEuropean Journal of Biochemistry, 1968
- Halogenation of tyrosine during acid hydrolysisBiochimica et Biophysica Acta, 1963