Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. Chymotrypsin catalyzes the hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues.
Stability/Storage: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder at 2-8°C. Protect from moisture.
Unit Definition: One Unit hydrolyzes one micromole of benzoyl-L-tyrosine ethyl ester per minute at 25°C, pH 7.8 in the presence of calcium. An activity of 45 units per mg using the above definition, is the equivalent of 10,000 optical density or 1330 N.F. units per mg using ATEE as a substrate.
Chymotrypsin, Alpha, TLCK Treated, Sequencing Grade
Three time crystallized and treated with 1-chloro-3-tosylamido-7-amino-2-heptanone (TLCK) to inhibit trypsin activity [Shaw, et al., Biochemistry, 4, 2219 (1965)]. Dialyzed to remove autolysis products and low molecular weight contaminants. Supplied as lyophilized powder.
Store at 2-8°C.
Chymotrypsin, Alpha, TLCK Treated
Three times crystallized and treated with 1-chloro-3-tosylamido-7-amino-2-heptanone (TLCK) to inhibit trypsin activity [Shaw, et al., Biochemistry, 4, 2219 (1965)]. Dialyzed against 1 mM HCl to remove autolysis products and low molecular weight contaminants. Supplied as a dialyzed, lyophilized powder.
Store at 2-8°C.
Chymotrypsin, Alpha, Purified
Chromatographically prepared by the procedure of Yapel, et al., J. Amer. Chem. Soc., 88, 2573 (1966). A lyophilized powder.
Store at 2-8°C.
Chymotrypsin, Alpha
Three times crystallized alpha chymotrypsin which is an activation product of a 3X crystallized zymogen. Dialyzed against 1mM HCl and lyophilized.
Store at 2-8°C.
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