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In this paper, the inhibitory kinetics of glabridin on tyrosinase and their binding mechanisms were determined using spectroscopic, zebrafish model and molecular docking techniques.
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Drug binding mechanisms were studied.
Stability, protein binding and logP values were determined.
K D values were determined using the 1 1 binding mechanism available in the Biacore evaluation software 4.1.
Together, these observations point to a general mechanism of cell-surface plg binding in which total binding is determined by the collective expression of a spectrum of heterogeneous receptors and proteolytic activity.
Phage titres were determined after binding between αUbi to rUbi and M13KO7 phage to rUbi.
Specificity and affinity were determined in cell binding studies.
Furthermore, clear evidence for the underlying binding mechanism is provided.
The dynamic binding capacity was determined.
HER2 binding affinity was determined in saturation radioligand binding assays using SKBR-3 cells (1.3 × 106 HER2/cell).
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