| 1. |
Kornberg, A. and Pricer, W. E., Jr. (1951b) Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J. Biol. Chem.
193, 481–495.
|
| |
| 2. |
Pfleiderer, G., Grein, L., and Wieland, T. (1955a) Specific determination of L-alanine and L-glutamine by means of glutamic-pyruvic transaminase. Ann. Acad. Sci. Fenn. Ser. A2, 60, 381–388.
|
| |
| 3. |
Pfleiderer, G., Gruber, W., and Wieland, T. (1955b) Eine enzymatische bestimmung der L-asparaginsäure. Biochem. Z.
326, 446–450.
|
| |
| 4. |
Kornberg, A. (1950) Reversible enzymatic synthesis of diphosphopyndine nucleotide and inorganic pyrophosphate. J. Biol. Chem.
182, 779–793.
|
| |
| 5. |
Moellering, H. and Gruber, G. (1966) Determination of citrate with citrate lyase. Anal. Biochem.
17, 369–376.
|
| |
| 6. |
Thorn, W., Pfleiderer, G., Frowein, R. A., and Ross, I. (1955) Stoffwechselvorgänge im Gehirn bei akuter Anoxie, akuter Ischämie
und in der Erholung. Pflueger’s Arch. Gesamte Physiol. Menschen Tiere
261, 334–360.
|
| |
| 7. |
Slein, M. W. (1950) Phosphomannose isomerase. J. Biol. Chem.
186, 753–761.
|
| |
| 8. |
Slater, E. C. (1953) Spectrophotometric determination of fructose-1∶6-diphosphate, hexose monophosphates, adenosinetriphosphate
and adenosine-diphosphate. Biochem. J.
53, 157–167.
|
| |
| 9. |
Vishniac, W. and Ochoa, S. (1952) Fixation of carbon dioxide coupled to photochemical reduction of pyridine nucleotides by
chloroplast preparations. J. Biol. Chem.
195, 75–96.
|
| |
| 10. |
Slein, M. W., Cori, G. T., and Cori, C. F. (1950) A comparative study of hexokinase from yeast and animal tissues. J. Biol. Chem.
186, 763–780.
|
| |
| 11. |
Paladini, A. C., Caputto, R., Leloir, L. F., Trucco, R. E., and Cardini, C. E. (1949) The enzymatic synthesis of glucose-1,6-diphosphate.
Arch. Biochem.
23, 55–66.
|
| |
| 12. |
Albers, R. W., Koval, G. McKahnn, G., and Ricks, D. (1961) in Regional Neurochemistry (Kety, S. S. and Elkes, J., eds.), Pergamon, Oxford, p. 340.
|
| |
| 13. |
Bublitz, C. and Kennedy, C. P. (1954) Synthesis of phosphatides in isolated mitochondria III. The enzymatic phosphorylation
of glycerol. J. Biol. Chem.
211, 951–961.
|
| |
| 14. |
Ochoa, S. (1948) Biosynthesis of tricarboxylic acids by carbon dioxide fixation. III. Enzymatic mechanisms. J. Biol. Chem.
174, 133–157.
|
| |
| 15. |
Noll, F. (1966) Methode zur Quantitativen Bestimmung von L(+)-Lactat mittels Lactat-Dehydrogenase und Glutamat-Pyruvate Transaminase. Biochem. Z.
346, 41–49.
|
| |
| 16. |
Kubowitz, F. and Ott, P. (1943) Isoliering und Kristallisation eines Gärungsfermente aus Tumoren. Biochem. Z.
314, 94–117.
|
| |
| 17. |
Strominger, J. L., Maxwell, E. S., and Kalckar, H. M. (1957) Meth. Enzymol.
3, 974.
|
| |
| 18. |
Strominger, J. L. (1955) Enzymic synthesis of guanosine and cytidine triphosphates: A note of the nucleotide specificity of
the pyruvate phosphokinase reaction. Biochim. Biophys. Acta
16, 616,617.
|
| |
| 19. |
Noda, L. and Kuby, S. A. (1963) Meth. Enzymol.
6, 223.
|
| |
| 20. |
Lowry, O. H., Schulz, D. W., and Passonneau, J. V. (1964) Effects of adenylic acid on the kinetics of muscle phosphorylase
a. J. Biol. Chem.
239, 1947–1953.
|
| |
| 21. |
Barbehenn, E. K., Law, M. M-Y., Brown, J. G., and Lowry, O. H. (1976) Measurement of 5′adenylic acid by stimulation of phosphorylase
a. Anal. Biochem.
70, 554–562.
|
| |
| 22. |
Lienhard, G. E. and Secemski, I. I. (1973) P1,P5-Di(adenosine-5′)penta-phosphate, a potent inhibitor of adenylate kinase. J. Biol. Chem.
248, 1121–1123.
|
| |
| 23. |
Lust, W. D., Feussner, G. K., Barbehenn, E. K., and Passonneau, J. V. (1981) The enzymatic measurement of adenine nucleotides
and P-creatine in picomole amounts. Anal. Biochem.
110, 258–266.
|
| |
| 24. |
Manchester, J. K., Chi, M. M.-Y., Carter, J., Pusateri, M. E., McDougal, D. B., and Lowry, O. H. (1990) Measurement of 2-deoxyglucose
and 2-deoxyglucose-6 phosphate in tissues. Anal. Biochem.
185, 118–124.
|
| |
| 25. |
Baranowski, T. (1963) in The Enzymes (Boyer, P. D., Lardy, H., and Myrback, K., eds.), rev. ed., vol. 7, Academic, New York, p. 63.
|
| |
| 26. |
Velick, S. F. and Furfine, C. (1963) in The Enzymes (Boyer, P. D., Lardy, H., and Myrbäck, K., eds.), vol. 7, Academic, New York, p. 243.
|
| |
| 27. |
Massey, V. and Alberty, R. A. (1964) Ionisation constants of fumarase. Biochim. Biophys. Acta
13, 354–359.
|
| |
| 28. |
Ray, W. J. Jr. and Roscelli, G. A. (1964) A kinetic study of the phosphoglucomutase pathway. J. Biol. Chem.
239, 1228–1236.
|
| |
| 29. |
Frieden, C. (1959a) Glutamic dehydrogenase II. The effect of various nucleotides on the association-dissociation and kinetic
properties. J. Biol. Chem.
234, 815–820.
|
| |
| 30. |
Frieden, C. (1959b) Glutamic dehydrogenase III. The order of substrate addition in the enzymatic reaction. J. Biol. Chem.
234, 2891–2896.
|
| |
| 31. |
Matschinsky, F. M. (1964) Personal communication.
|
| |
| 32. |
Passonneau, J. V. and Lauderdale, V. R. (1974) A comparison of three methods of glycogen measurement in tissues. Anal. Biochem.
60, 405–412.
|
| |
| 33. |
Lust, W. D., Passonneau, J. V., and Crites, S. K. (1975) The measurement of glycogen in tissues by amylo-α-1,4-α-1,6-glucosidase
after the destruction of preexisting glucose. Anal. Biochem.
68, 128–131.
|
| |
| 34. |
Passonneau, J. V. and Rottenberg, D. A. (1973) An assessment of methods for measurement of glycogen synthetase activity including
a new direct one-step assay. Anal. Biochem.
51, 405–412.
|
| |
| 35. |
de Azeredo, F. A. M., Feussner, G. K., Lust, W. D., and Passonneau, J. V. (1979) An enzymatic method for the measurement of
GTP and GDP in biological samples. Anal. Biochem.
95, 512–519.
|
| |
| 36. |
Kaufman, F. and Alivisatos, S. G. A. (1955) Purification and properties of the phosphorylating enzyme from spinach. J. Biol. Chem.
216, 141–152.
|
| |
| 37. |
Cha, S. and Parks, J. E., Jr. (1964) Succinic thiokinase. II Kinetic studies; initial velocity, product inhibition, and effect
of arsenate. J. Biol. Chem.
239, 1968–1977.
|
| |
| 38. |
Olson, J. A. and Anfinsen, C. B. (1953) Kinetic and equilibrium studies on crystalline L-glutamic acid dehydrogenase. J. Biol. Chem.
202, 841–856.
|
| |
| 39. |
Hintz, C. S., Chi, M. M.-Y., Fell, R. D., Ivy, J. L., Kaiser, K. K., Lowry, C. V., and Lowry, O. H. (1982) Metabolite changes
in individual rat muscle fibers during stimulation. Am. J. Physiol.
242, C218–C228.
|
| |
| 40. |
Krebs, H. A. (1953) Equilibria in transamination systems. Biochem. J.
54, 82–86.
|
| |
| 41. |
Fawaz, E. N., Roth, L., and Fawaz, G. (1966) The enzymatic estimation of inorganic phosphate. Biochem. Z.
344, 212–214.
|
| |
| 42. |
Pontremoli, S., de Flora, A., Grazi, E., Mangiarotta, G., Bonsignore, A., and Horecker, B. L. (1961) Crystalline D-gluconate-6-phosphate dehydrogenase. J. Biol. Chem.
236, 2975–2980.
|
| |
| 43. |
Outlaw, W. H., Jr. and Lowry, O. H. (1979) Measurement of 10−7 to 10−12 mol of potassium by stimulation of pyruvate kinase. Anal. Biochem.
92, 370–374.
|
| |
| 44. |
Cook, G. A., O’Brien, W. E., Wood, H. G., King, M. T., and Veech, R. L. (1978) A rapid, enzymatic assay for the measurement
of inorganic pyrophosphate in animal tissues. Anal. Biochem.
91, 557–565.
|
| |
| 45. |
Jones, M. G. K., Outlaw, W. H., Jr., and Lowry, O. H. (1977) Enzymic assay of 10−7 to 10−14 moles of sucrose in plant tissues. Plant Physiol.
60, 379–383.
|
| |