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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
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12 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  0.598
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  0.576
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  0.338
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  0.309
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  0.643
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  0.652
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  0.667
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  0.64
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  0.532
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. DOI: 10.1016/0006-291X(66)90668-1  0.615
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.  0.355
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  0.522
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