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1 subsequently was enzymatically digested with alpha-chymotrypsin.
2 face of the enzyme protein bovine pancreatic alpha-chymotrypsin.
3 he dielectric response in the active site of alpha-chymotrypsin.
4 isolated following limited proteolysis with alpha-chymotrypsin.
5 eating the denatured protein with trypsin or alpha-chymotrypsin.
6 tion with endoproteinase Asp-N, trypsin, and alpha-chymotrypsin.
7 vex Eyring plots that have been observed for alpha-chymotrypsin (alpha-CT)-catalyzed hydrolysis of sp
8 we determine the rate of E*I* formation from alpha-chymotrypsin and alpha1-antichymotrypsin using two
13 tween TH-1 and TH-2/3 is cleaved by trypsin, alpha-chymotrypsin, and endo-AspN but not V8 protease.
14 nd 12 are strongly hydrophobic, resistant to alpha-chymotrypsin, and retained by the membrane bilayer
15 cells with proteases (proteinase K, papain, alpha-chymotrypsin, and trypsin) abrogated entry, indica
16 ested with two serine proteases, trypsin and alpha-chymotrypsin, and two serine esterases, acetylchol
17 lbicans; the serine proteases granzyme B and alpha-chymotrypsin; and the cysteine proteases cathepsin
18 this approach, the activities of trypsin and alpha-chymotrypsin are detected using protamine and synt
24 ndencies and solvent isotope effects for the alpha-chymotrypsin-catalyzed hydrolysis of Suc-Phe-pNA (
26 clusters modulate the catalytic behavior of alpha-chymotrypsin (ChT) toward cationic, neutral, and a
27 The interaction of these nanoparticles with alpha-chymotrypsin (ChT) was investigated by activity as
28 thermodynamics of these functional NPs with alpha-chymotrypsin (ChT), histone, and cytochrome c (Cyt
29 protein isolate (WPI) were hydrolysed using alpha-chymotrypsin (chymotrypsin), pepsin and trypsin.
30 human erythrocytes with trypsin, followed by alpha-chymotrypsin, cleaved Kx and destroyed the binding
35 ted enzymatic hydrolysis was performed using alpha-chymotrypsin immobilised on agarose microparticles
36 time is 3h, the limit of detection (LOD) for alpha-chymotrypsin in buffer solution is 50 ng/mL, where
37 basis of the dark or bright signal from LC, alpha-chymotrypsin in buffer solution or complex media s
38 ng limited proteolysis with either papain or alpha-chymotrypsin indicated that the amino acid accepto
40 nique dual-function peptide, i.e. a specific alpha-chymotrypsin inhibitor and a potent tumorigenesis/
41 er was sufficient to reduce both trypsin and alpha-chymotrypsin inhibitors to negligible values, also
42 e ectodomain of gB, gB(730t), was cleaved by alpha-chymotrypsin into two major fragments comprising a
43 acellular Na(+), mechanical shear stress, or alpha-chymotrypsin-mediated proteolysis, suggesting that
44 d to determine the in vitro conformations of alpha-chymotrypsin oligomers that form as a result of pa
45 ittle difference between active and inactive alpha-chymotrypsin, only active protease can be detected
46 proteolysis of the recombinant protein with alpha-chymotrypsin produced four discrete fragments reve
48 atment of peanuts by ultrasonication-trypsin-alpha chymotrypsin, resulted in maximum reductions of Ar
49 K) and RDMQDMEFTIEEGKL (positions 317-331 in alpha-chymotrypsin-treated PPDK), thus locating one of t
50 ydrolyze substrates for thrombin, factor Xa, alpha-chymotrypsin, trypsin, or plasmin, nor did it immu
51 Screening this library with biotinylated alpha-chymotrypsin under appropriate conditions revealed
53 luorescent change resulting from reaction of alpha-chymotrypsin with a fluorescent derivative of alph