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Alkaline denaturation and partial refolding of pepsin investigated with DAPI as an extrinsic probe.
Favilla R, Parisoli A, Mazzini A. Favilla R, et al. Among authors: mazzini a. Biophys Chem. 1997 Sep 1;67(1-3):75-83. doi: 10.1016/s0301-4622(97)00016-1. Biophys Chem. 1997. PMID: 9397520
The binding parameters of DAPI to porcine stomach pepsin have been described in the previous article in this issue (A. Mazzini et al.). Here we exploit the differences in the spectroscopic (fluorescence and circular dichroism) properties of DAPI bound to either nati …
The binding parameters of DAPI to porcine stomach pepsin have been described in the previous article in this issue (A. Mazzini
The binding of 4',6-diamidino-2-phenylindole to bovine serum albumin.
Mazzini A, Cavatorta P, Iori M, Favilla R, Sartor G. Mazzini A, et al. Biophys Chem. 1992 Jan;42(1):101-9. doi: 10.1016/0301-4622(92)80012-t. Biophys Chem. 1992. PMID: 1581510
The binding of 4',6-diamidino-2-phenylindole (DAPI) to bovine serum albumin (BSA) has been investigated between pH 6 and 8, in 0.05 M phosphate buffer at 20 degrees C, by fluorescence titrations and the results analyzed according to a procedure previously reported (R. Favi …
The binding of 4',6-diamidino-2-phenylindole (DAPI) to bovine serum albumin (BSA) has been investigated between pH 6 and 8, in 0.05 M phosph …
Interaction of DAPI with pepsin as a function of pH and ionic strength.
Mazzini A, Incerti M, Favilla R. Mazzini A, et al. Biophys Chem. 1997 Sep 1;67(1-3):65-74. doi: 10.1016/s0301-4622(97)00015-x. Biophys Chem. 1997. PMID: 9397519
Fluorescence and CD titrations show that nearly two molecules of DAPI bind to either native or alkali denatured pepsin with pH and ionic strength dependent Kd values, whereas absorbance titrations evidentiate an interaction characterized by a lower affinity and a la …
Fluorescence and CD titrations show that nearly two molecules of DAPI bind to either native or alkali denatured pepsin with pH and ionic str …
57 results