The nature of the enzyme blank observed with crystalline α-chymotrypsin
- 31 December 1957
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta
- Vol. 26 (3) , 634-635
- https://doi.org/10.1016/0006-3002(57)90110-5
Abstract
No abstract availableKeywords
This publication has 5 references indexed in Scilit:
- The Empirical Evaluation of the Initial Velocities of Enzyme-catalyzed Reactions1Journal of the American Chemical Society, 1956
- Re-evaluation of the Inhibition Constants of Previously Investigated Competitive Inhibitors of α-Chymotrypsin. II. Mono-, Bi- and Trifunctional Inhibitors Evaluated under Zone A Conditions1Journal of the American Chemical Society, 1955
- Re-evaluation of the Inhibition Constants of Previously Investigated Competitive Inhibitors of α-Chymotrypsin. I. Hydrolysis Products and Enantiomorphs of Previously Investigated Specific Substrates1Journal of the American Chemical Society, 1955
- Re-evaluation of the Kinetic Constants of Previously Investigated Specific Substrates of α-Chymotrypsin1Journal of the American Chemical Society, 1955
- Automatic Recording pH InstrumentationAnalytical Chemistry, 1955