A rapid preparation of the apo—holo hybrid of aspartate aminotransferase

[1]  G. Eichele,et al.  The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 A resolution. , 1979, Journal of molecular biology.

[2]  J. Tenu,et al.  Inorganic phosphate binding to apoaspartate aminotransferase , 1979, FEBS letters.

[3]  B. Vainshtein,et al.  Three-dimensional structure at 5 A resolution of cytosolic aspartate transaminase from chicken heart. , 1978, Journal of molecular biology.

[4]  P. Christen,et al.  Aspartate aminotransferase. Determination of the active site occupancy pattern indicates independent transamination of the two subunits. , 1977, The Journal of biological chemistry.

[5]  M. Martinez‐Carrion,et al.  Itemizing enzyme ligand interactions in native and and half-active hybrid aspartate transaminase to probe site-site relationships. , 1976, Biochemistry.

[6]  M. Goldberg,et al.  Structural and functional interdependence of the protomers of Escherichia coli K 12 tryptophanase during binding of pyridoxal 5'-phosphate. , 1976, Journal of Biological Chemistry.

[7]  H. Zeisel,et al.  Complementation of subunits from glycogen phosphorylases of frog and rabbit skeletal muscle and rabbit liver. , 1976, European journal of biochemistry.

[8]  I. Cournil,et al.  Dissociation of aspartate aminotransferase into subunits. Effect of ligands upon this dissociation. , 1975, The Journal of biological chemistry.

[9]  H. K. Schachman,et al.  Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[10]  M. Martinez‐Carrion,et al.  Hybridization of glutamate aspartate transaminase. Investigation of subunit interaction. , 1975, Biochemistry.

[11]  Y. Lee,et al.  Mitochondrial aspartate aminotransferase-independent function of the catalytic binding sites. , 1975, The Journal of biological chemistry.

[12]  I. Cournil,et al.  Interactions between aspartate animotransferase protomers observed during holoenzyme reconstitution.. , 1975, Biochemical and biophysical research communications.

[13]  J. Holbrook,et al.  Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-phosphate. , 1974, Biochemical Journal.

[14]  P. Christen,et al.  The apo-holo hybrid of cytosolic aspartate aminotransferase, preparation and studies on subunit interactions. , 1974, Biochemical and biophysical research communications.

[15]  P. Christen,et al.  The reactive sulfhydryl groups of cytoplasmic aspartate aminotransferase. Localization in the primary structure and spectral properties of their mixed disulfide derivatives with N-dansylcysteine. , 1974, European journal of biochemistry.

[16]  V. Nosikov,et al.  Location of exposed and buried cysteine residues in the polypeptide chain of aspartate aminotransferase , 1973, FEBS letters.

[17]  P. Christen,et al.  Cytoplasmic aspartate aminotransferase: syncatalytic sulfhydryl group modification. , 1973, The Journal of biological chemistry.

[18]  M. Arrio-Dupont.  Interaction between pyridoxamine 5'-phosphate and apo-aspartate aminotransferase from pig heart. Evidence for a negative cooperativity. , 1972, European journal of biochemistry.

[19]  P. Fottrell,et al.  Interactions between an unusual aspartate aminotransferase from Rhizobium japonicum and pyridoxal‐5′‐phosphate studied by affinity chromatography , 1972, FEBS Letters.

[20]  H. K. Schachman,et al.  Hybridization of native and chemically modified enzymes. I. Development of a general method and its application to the study of the subunit structure of aldolase. , 1970, Biochemistry.

[21]  M. Martinez‐Carrion,et al.  Mitochondrial aspartate transaminase. II. Isolation and characterization of the multiple forms. , 1969, Biochemistry.

[22]  I. Crawford,et al.  Subunit structure of the B component of Escherichia coli tryptophan synthetase. , 1969, Biochemistry.

[23]  P. Fasella,et al.  Isolation and characterization of multiple forms of glutamate-asparate aminotransferase from pig heart. , 1967, The Journal of biological chemistry.

[24]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[25]  H. Wada,et al.  Enzymatic transamination of pyridoxamine. I. With oxaloacetate and alpha-ketoglutarate. , 1962, The Journal of biological chemistry.