S. Kuby

发表

Studies on adenosine triphosphate transphosphorylases. IX. Kinetic properties of the crystalline adenosine triphosphate-creatine transphosphorylase from calf brain.

H. Jacobs, S. Kuby, 1970, The Journal of biological chemistry.

Glucose-6-phosphate dehydrogenase from brewers' yeast. The effects of pH and temperature on the steady-state kinetic parameters of the two-chain protein species.

S. Kuby, R. Roy, 1976, Biochemistry.

Glucose 6-phosphate dehydrogenase (Zwischenferment). II. Homogeneity measurements and physical properties of the crystalline apoenzyme from yeast.

E. Noltmann, S. Kuby, R. Yue, 1967, Biochemistry.

Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase.

L. H. Wu, S. Kuby, R. Palmieri, 1984, Biochemistry.

NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme.

A. Mildvan, D. Fry, S. Kuby, 1985, Biochemistry.

Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase.

E. Noltmann, S. Kuby, T. A. Mahowald, 1962, The Journal of biological chemistry.

Adenosinetriphosphate-creatine transphosphorylase. II. Homogeneity and physicochemical properties.

H. Lardy, S. Kuby, L. Noda, 1954, The Journal of biological chemistry.

Properties of Thiolesters: Kinetics of Hydrolysis in Dilute Aqueous Media1

H. Lardy, S. Kuby, L. Noda, 1953 .

Studies on adenosine triphosphate transphosphorylases. XVII. A physicochemical comparison of the ATP-creatine transphosphorylase (creatine kinase) isozymes from man, calf, and rabbit

K. Okabe, S. Kuby, R. Yue, 1983 .

Studies on adenosine triphosphate transphosphorylases. 8. Homogeneity and physicochemical properties of the crystalline adenosine triphosphate--creatine transphosphorylase from calf brain.

K. Okabe, H. Jacobs, S. Kuby, 1968, Biochemistry.

[100] ATP-Creatine transphosphorylase: ATP+Cr⇋ADP+Cr∼P

H. Lardy, S. Kuby, L. Noda, 1955 .

Adenosinetriphosphate-creatine transphosphorylase. III. Kinetic studies.

H. Lardy, S. Kuby, L. Noda, 1954, The Journal of biological chemistry.

Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle.

H. Lardy, S. Kuby, L. Noda, 1954, The Journal of biological chemistry.

Purification and Kinetics of β-D-Galactosidase from Escherichia coli, Strain K-121,2

H. Lardy, S. Kuby, 1953 .

Adenosine triphosphate-adenosine-5'-monophosphate phosphotransferase from normal human liver mitochondria. Isolation, chemical properties, and immunochemical comparison with Duchenne dystrophic serum aberrant adenylate kinase.

T. Watanabe, H. Okuda, M. Sumida, 1982, The Journal of biological chemistry.

Adenosinetriphosphate-creatine transphosphorylase. IV. Equilibrium studies.

H. Lardy, S. Kuby, L. Noda, 1954, The Journal of biological chemistry.

Isolation of the human ATP-creatine transphosphorylases (creatine phosphokinases) from tissues of patients with Duchenne muscular dystrophy.

F. H. Tyler, K. Okabe, H. Jacobs, 1977, The Journal of biological chemistry.

Studies on adenosine triphosphate transphosphorylases. XI. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylases from the muscle and brain of man, calf, and rabbit; and a preparation of their enzymatically active hybrids.

K. Okabe, H. Jacobs, F. Ziter, 1978, Archives of biochemistry and biophysics.

Studies on adenosine triphosphate transphosphorylases. IV. Enzyme-substrate interactions.

E. Noltmann, S. Kuby, T. A. Mahowald, 1962, Biochemistry.

Multiforms of mammalian adenylate kinase and its monoclonal antibody against AK1.

H. Takenaka, M. Sumida, M. Hamada, 1990, Enzyme.

NUCLEOSIDE TRIPHOSPHATE-NUCLEOSIDE DIPHOSPHATE TRANSPHOSPHORYLASE (NUCLEOSIDE DIPHOSPHOKINASE). I. ISOLATION OF THE CRYSTALLINE ENZYME FROM BREWERS' YEAST.

R. Ratliff, H. Lardy, S. Kuby, 1973, The Journal of biological chemistry.

Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). II. Homogeneity measurements and physicochemical properties.

S. Kuby, L. Noda, 1957, The Journal of biological chemistry.

Glucose 6-phosphate dehydrogenase from brewers' yeast (Zwischenferment). 3. Studies on the subunit structure and on the molecular association phenomenon induced by triphosphopyridine nucleotide.

E. Noltmann, S. Kuby, R. Yue, 1969, The Journal of biological chemistry.

Studies on adenosine triphosphate transphosphorylases. XVIII. Synthesis and preparation of peptides and peptide fragments of rabbit muscle ATP-AMP transphosphorylase (adenylate kinase) and their nucleotide-binding properties

D. Bredt, A. Mildvan, Mark S. Johnson, 1989 .

Studies on adenosine triphosphate transphosphorylases. XIII. Kinetic properties of the crystalline rabbit muscle ATP-AMP transphorphorylase (adenylate kinase) and a comparison with the crystalline calf muscle and liver adenylate kinases.

M. Hamada, S. Kuby, 1978, Archives of biochemistry and biophysics.

Studies on NADH(NADPH)-cytochrome c reductase (FMN-containing) from yeast: steady-state kinetic properties of the flavoenzyme from top-fermenting ale yeast.

M. S. Johnson, S. Kuby, 1986, Archives of biochemistry and biophysics.

Glucose 6-phosphate dehydrogenase from brewers' yeast (Zwischenferment). Further observations on the ligand-induced macromolecular association phenomenon: kinetic properties of the two-chain protein species; and studies on the enzyme-substrate interactions.

J. Wu, S. Kuby, R. Roy, 1974, Archives of biochemistry and biophysics.

An aberrant adenylate kinase isoenzyme from the serum of patients with Duchenne muscular dystrophy.

F. H. Tyler, T. Watanabe, H. Okuda, 1981, Biochimica et biophysica acta.

Studies on muscular dystrophy: a comparison by physical and chemical means of the normal human ATP-creatine transphosphorylases (creatine kinases) with those from tissues of Duchenne muscular dystrophy.

K. Okabe, S. Kuby, R. Palmieri, 1979, Archives of biochemistry and biophysics.

Solution structure of the 45-residue MgATP-binding peptide of adenylate kinase as examined by 2-D NMR, FTIR, and CD spectroscopy.

A. Mildvan, D. Fry, H. Susi, 1986, Biochemistry.

ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins.

A. Mildvan, D. Fry, D C Fry, 1986, Proceedings of the National Academy of Sciences of the United States of America.

A Study of enzymes

S. Kuby, 1990 .

Studies on adenosine triphosphate transphosphorylases. III. Inhibition reactions.

E. Noltmann, S. Kuby, T. A. Mahowald, 1962, The Journal of biological chemistry.

Studies on Adenosine Triphosphate Transphosphorylases

E. Noltmann, S. Kuby, T. A. Mahowald, 2001 .

A steady-state kinetic analysis of the prolyl-4-hydroxylase mechanism.

N. Soskel, S. Kuby, 1981, Connective tissue research.

Rabbit muscle creatine phosphokinase. CDNA cloning, primary structure and detection of human homologues.

W. Herlihy, K. Biemann, H. Pang, 1984, The Journal of biological chemistry.

[23] Glucose 6-phosphate dehydrogenase (crystalline) from brewers' yeast

E. Noltmann, S. Kuby, 1966 .

Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast.

E. Noltmann, E A NOLTMANN, C J GUBLER, 1961, The Journal of biological chemistry.

Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). I. Isolation of the crystalline enzyme from rabbit skeletal muscle.

S. Kuby, L. Noda, 1957, The Journal of biological chemistry.

Studies on adenosine triphosphate transphophorylases. V. Studies on the polypeptide chains of the crystalline adenosine triphosphate-creatine transphosphorylase from rabbit skeletal muscle.

S. Kuby, R. Yue, R. Palmieri, 1967, Biochemistry.

STUDIES ON ADENOSINE TRIPHOSPHATE-ADENOSINE TRIPHOSPHATE TRANSPHOSPHORYLASES. V. CARBOXYL-TERMINAL SEQUENCES OF ADENOSINE TRIPHOSPHATE-CREATINE TRANSPHOSPHORYLASE AND OF ADENOSINE 5'-PHOSPHATE TRANSPHOSPHORYLASE (MYOKINASE).

S. Kuby, O. Olson, 1964, The Journal of biological chemistry.

Partial purification and properties of thiamine pyrophosphokinase from pig brain.

S. Kuby, C. Gubler, J. W. Peterson, 1975, Biochimica et biophysica acta.

PURIFICATION AND KINETIC PROPERTlES OF PORCINE THIAMlN PYROPHOSPHOKINASE *

S. Kuby, C. Gubler, G. Fleming, 1982 .

Studies of adenosine triphosphate transphosphorylases. XIV. Equilibrium binding properties of the crystalline rabbit and calf muscle ATP--AMP transphosphorylase (adenylate kinase) and derived peptide fragments.

M. Hamada, S. Kuby, R. Palmieri, 1979, Archives of biochemistry and biophysics.

Systems for the separation of phosphoric esters by solvent distribution.

G. Plaut, H. Lardy, S. Kuby, 1950, The Journal of biological chemistry.

Studies on adenosine triphosphate transphosphorylases. Human isoenzymes of adenylate kinase: isolation and physicochemical comparison of the crystalline human ATP-AMP transphosphorylases from muscle and liver.

M. Hamada, S. Kuby, A. Frischat, 1983, The Journal of biological chemistry.

Studies on adenosine triphosphate transphosphorylases. Isolation and several properties of the crystalline calf ATP-AMP transphosphorylases (adenylate kinases) from muscle and liver and some observations on the rabbit muscle adenylate kinase.

L. H. Wu, M. Hamada, H. Jacobs, 1978, Archives of biochemistry and biophysics.

Studies on adenosine triphosphate transphosphorylases. I. Amino acid composition of adenosine triphosphate-adenosine 5'-phosphate transphosphorylase (myokinase).

E. Noltmann, S. Kuby, T. A. Mahowald, 1962, The Journal of biological chemistry.

Rabbit Muscle Creatine Phosphokinase

S. Kuby, Paul Schimmels, Nancy Royall, 1984 .

Nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). II. Physical properties of the crystalline enzyme from brewers' yeast.

R. Ratliff, S. Kuby, R. Yue, 1967, Biochemistry.

Studies on NADPH-cytochrome c reductase I: Isolation and several properties of the crystalline enzyme from ale yeast.

M. Hamada, S. Kuby, M. C. Cress, 1979, Archives of biochemistry and biophysics.

In vitro mutagenesis studies at the arginine residues of adenylate kinase. A revised binding site for AMP in the X-ray-deduced model.

H. J. Kim, S. Nishikawa, H. Takenaka, 1990, Biochemistry.

NMR studies of the AMP-binding site and mechanism of adenylate kinase.

A. Mildvan, D. Fry, S. Kuby, 1986, Biochemistry.

Synthetic genes for human muscle-type adenylate kinase in Escherichia coli.

H. J. Kim, S. Nishikawa, H. Takenaka, 1989, Protein engineering.

Crystalline Beef Cytochrome c.

B. Thorell, K. Paul, H. Theorell, 1956 .

Purification and Kinetics of beta - delta-Galactosidase from Escherichia coli, Strain K-12 - Correction

H. Lardy, S. Kuby, 1953 .

Effects of pH and Temperature

S. Kuby, 2019, A Study of Enzymes: Volume I Enzyme Catalysis, Kinetics, and Substrate Binding.

Studies on adenosine triphosphate transphosphorylases. VII. Isolation of the crystalline adenosine triphosphate--creatine transphosphorylase from calf brain.

K. Okabe, H. Jacobs, S. Kuby, 1968, Biochemistry.

[27] Myokinase, ATP-AMP transphosphorylase: 2ADP ⇄ ATP + AMP

S. Kuby, L. Noda, 1963 .

Studies on the adenylate kinase isozymes from the serum and erythrocyte of normal and Duchenne dystrophic patients. Isolation, physicochemical properties, and several comparisons with the Duchenne dystrophic aberrant enzyme.

T. Watanabe, H. Okuda, M. Sumida, 1985, Journal of Biological Chemistry.

Studies on NADH (NADPH)-cytochrome c reductase (FMN-containing) from yeast. Isolation and physicochemical properties of the enzyme from top-fermenting ale yeast.

S. Kuby, M. S. Johnson, 1985, The Journal of biological chemistry.