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
ON THE REACTION OF ACETAMIDOMETHANOL WITH NATIVE AND REDUCED BOVINE PANCREATIC TRYPSIN INHIBITOR (KUNITZ INHIBITOR)
β Scribed by Rocchi, Raniero ;Benassi, Carlo A. ;Tomatis, Roberto ;Ferroni, Roberto ;Menegatti, Enea
- Book ID
- 115097220
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 541 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0367-8377
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Collision cross sections have been measured for gas phase ions of native oxidized bovine pancreatic trypsin inhibitor (BPTI), native reduced BPTI and a mutant form of BPTI containing a single disulphide bond between residues 5 and 55 ([5-55] Ala BPTI). Cross sections for [5-55] Ala BPTI and reduced
## Abstract Values of the association equilibrium constant (__K__~a~) for the binding of the native and of the cyanogen bromideβcleaved bovine basic pancreatic trypsin inhibitor (native BPTI and [Hse lactoneβ52]β52,53β__seco__βBPTI, respectively) to neuraminidaseβtreated porcine pancreatic Ξ²βKallik