Karl G. Brandt
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=5Google:
"Karl G. Brandt"Bio:
http://chemistry.library.nd.edu/resources/genealogy/chemistry/documents/BrandtKG.pdf
Mean distance: 8.07 | S | N | B | C | P |
Parents
Sign in to add mentor| John Clark Sheehan | grad student | 1964 | MIT | |
| (Monocyclic penicillin analogs) | ||||
| George Paul Hess | post-doc | 1966 | Cornell | |
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Publications
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| Huber PW, Brandt KG. (1985) Kinetic studies of the reduction of yeast glutathione reductase by reduced nicotinamide hypoxanthine dinucleotide phosphate. Archives of Biochemistry and Biophysics. 238: 213-8 |
| Huber PW, Brandt KG. (1980) Kinetic studies of the mechanism of pyridine nucleotide dependent reduction of yeast glutathione reductase. Biochemistry. 19: 4569-75 |
| Moroff G, Brandt KG. (1975) 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 |
| Moroff G, Brandt KG. (1973) Steady-state kinetic investigation of specific anion effects on the catalytic activity of yeast glutathione reductase. Archives of Biochemistry and Biophysics. 159: 468-74 |
| McConn J, Ku E, Himoe A, et al. (1971) 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 |
| Himoe A, Brandt KG, DeSa RJ, et al. (1969) 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 |
| Brandt KG, Himoe A, Hess GP. (1967) 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 |
| Himoe A, Brandt KG, Hess GP. (1967) 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 |
| Brandt KG, Parks PC, Czerlinski GH, et al. (1966) 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 |
| Brandt KG, Hess GP. (1966) 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 |