Add time:09/04/2019         Source:sciencedirect.com

Conjugation of trypsin and TRYPSIN INHIBITOR (cas 12786-39-9) with milk beta-lactoglobulin (b-LG) was studied in aqueous solution at physiological pH. Multiple spectroscopic methods and transmission electron microscopy (TEM) were used to characterize protein–protein interactions and protein morphology. Thermodynamic analysis ΔH (−24 to −11 kJ Mol−1), ΔS (−30 to −5 J Mol−1 K−1) and ΔG (−12 to −10 kJ Mol−1) showed that protein–protein interactions occur via H-bonding and van der Waals contacts. The binding affinity was trypsin > trypsin inhibitor with Ktrypsin-b-LG = 9.8 (±1) × 104 M−1 and Ktrypsininhibitor-b-LG = 7.5 (±0.7) x 103M−1. Transmission electron microscopy showed major changes in protein morphology upon protein–protein interactions.

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