Karl G. Brandt - Publications

Affiliations: 
Biochemistry Purdue University, West Lafayette, IN, United States 
Website:
http://e-archives.lib.purdue.edu/cdm4/item_viewer.php?CISOROOT=/oralhist&CISOPTR=143&CISOBOX=1&REC=5

20 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1985 Huber PW, Brandt KG. Kinetic studies of the reduction of yeast glutathione reductase by reduced nicotinamide hypoxanthine dinucleotide phosphate. Archives of Biochemistry and Biophysics. 238: 213-8. PMID 3885856 DOI: 10.1016/0003-9861(85)90158-4  1
1985 Sherban DG, Kennelly PJ, Brandt KG, Rodwell VW. Rat liver 3-hydroxy-3-methylglutaryl-CoA reductase. Catalysis of the reverse reaction and two half-reactions. The Journal of Biological Chemistry. 260: 12579-85. PMID 2413027  1
1984 Harwood HJ, Brandt KG, Rodwell VW. Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates. The Journal of Biological Chemistry. 259: 2810-5. PMID 6698994  1
1983 Kennelly PJ, Brandt KG, Rodwell VW. 3-hydroxy-3-methylglutaryl-CoA reductase: solubilization in the presence of proteolytic inhibitors, partial purification, and reversible phosphorylation-dephosphorylation. Biochemistry. 22: 2784-8. PMID 6307348 DOI: 10.1021/Bi00281A002  1
1980 Huber PW, Brandt KG. Kinetic studies of the mechanism of pyridine nucleotide dependent reduction of yeast glutathione reductase. Biochemistry. 19: 4569-75. PMID 7000180 DOI: 10.1021/Bi00561A005  1
1976 Moroff G, Ochs RS, Brandt KG. Yeast glutathione reductase. Steady-state kinetic studies of its transhydrogenase activity. Archives of Biochemistry and Biophysics. 173: 42-9. PMID 4035 DOI: 10.1016/0003-9861(76)90232-0  1
1975 Moroff G, Brandt KG. Yeast glutathione reductase. Studies of the kinetics and stability of the enzyme as a function of pH and salt concentration. Biochimica Et Biophysica Acta. 410: 21-31. PMID 74 DOI: 10.1016/0005-2744(75)90204-1  1
1973 Moroff G, Brandt KG. Steady-state kinetic investigation of specific anion effects on the catalytic activity of yeast glutathione reductase. Archives of Biochemistry and Biophysics. 159: 468-74. PMID 4593816 DOI: 10.1016/0003-9861(73)90476-1  1
1971 McConn J, Ku E, Himoe A, Brandt KG, Hess GP. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. V. Determination of pre-steady state kinetic parameters for specific substrate esters by stopped flow techniques. The Journal of Biological Chemistry. 246: 2918-25. PMID 5554299  1
1971 Rogers MJ, Brandt KG. Multiple inhibition analysis of Aspergillus niger glucose oxidase by D-glucal and halide ions. Biochemistry. 10: 4636-41. PMID 5140182  1
1971 Rogers MJ, Brandt KG. Interaction of halide ions with Aspergillus niger glucose oxidase. Biochemistry. 10: 4630-5. PMID 5140181  1
1971 Rogers MJ, Brandt KG. Interaction of D-glucal with Aspergillus niger glucose oxidase. Biochemistry. 10: 4624-30. PMID 5140180  1
1971 Bulger JE, Brandt KG. Yeast glutathione reductase. II. Interaction of oxidized and 2-electron reduced enzyme with reduced and oxidized nicotinamide adenine dinucleotide phosphate. The Journal of Biological Chemistry. 246: 5578-87. PMID 4398525  1
1971 Bulger JE, Brandt KG. Yeast glutathione reductase. I. Spectrophotometric and kinetic studies of its interaction with reduced nicotinamide adenine dinucleotide. The Journal of Biological Chemistry. 246: 5570-7. PMID 4398524  1
1969 Himoe A, Brandt KG, DeSa RJ, Hess GP. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. IV. Pre-steady state kinetic approaches to the investigation of the catalytic hydrolysis of esters. The Journal of Biological Chemistry. 244: 3483-93. PMID 5798622  1
1967 Brandt KG, Himoe A, Hess GP. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. 3. Determination of individual rate constants and enzyme-substrate binding constants for specific amide and ester substrates. The Journal of Biological Chemistry. 242: 3973-82. PMID 6037555  1
1967 Himoe A, Brandt KG, Hess GP. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. II. Characterization of the spectral changes of the enzyme at 290 m-mu and determination of over-all enzyme-substrate dissociation constants. The Journal of Biological Chemistry. 242: 3963-72. PMID 6037554  1
1966 Brandt KG, Parks PC, Czerlinski GH, Hess GP. On the elucidation of the pH dependence of the oxidation-reduction potential of cytochrome c at alkaline pH. The Journal of Biological Chemistry. 241: 4180-5. PMID 4958912  1
1966 Brandt KG, Hess GP. Determination of the binding constant of a specific ester and a specific amide substrate to α-chymotrypsin Biochemical and Biophysical Research Communications. 22: 447-452.  1
1965 Sheehan JC, Brandt KG. A novel cleavage of the penicillin nucleus. Journal of the American Chemical Society. 87: 5468-9. PMID 5844823 DOI: 10.1021/Ja00951A038  0.88
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