The kinetics of the formation of the complex between bovine P-trypsin and the bovine basic pancreatic trypsin inhibitor (BPTI) was investigated using three different signals: the displacement of proflavine, the optical density changes in the UV region, and the loss of the enzymatic activity. For the
β¦ LIBER β¦
The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
β Scribed by R. Huber; W. Bode; D. Kukla; U. Kohl; C. A. Ryan
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 553 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1432-1017
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Fourier transform infrared (FTIR) spectroscopy combined with resolution enhancement techniques, second-derivative and difference spectroscopies, have been used to characterize pressure-induced changes in the structural rearrangements of bovine pancreatic trypsin inhibitor (BPTI) in D 2 O solution at