Stability studies on derivatives of the bovine pancreatic trypsin inhibitor
โ Scribed by Schwarz, Herbert; Hinz, Hans Juergen; Mehlich, Armin; Tschesche, Harald; Wenzel, Herbert R.
- Book ID
- 126323021
- Publisher
- American Chemical Society
- Year
- 1987
- Tongue
- English
- Weight
- 891 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-2960
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๐ SIMILAR VOLUMES
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
The kinetics of the formation of the complex between bovine P-trypsin and the porcine pancreatic secretory trypsin inhibitor (PSTI; Kaza-type inhibitor) was investigated following the spectral changes associated with the displacement of proflavine from the enzyme, upon inhibitor binding, between pH