Chymotrypsin, Alpha, 3x cryst., TLCK treated – CDTLCK

Description

Chymotrypsin is a serine endopeptidase produced by the acinar cells of the pancreas. Chymotrypsin becomes activated after proteolysis of chymotrypsinogen by trypsin. While trypsin hydrolyzes at lysine and arginine, chymotrypsin selectively cleaves peptide bonds formed by aromatic residues (tyrosine, phenylalanine, and tryptophan) (Hedstrom et al. 1992). Two predominant forms of chymotrypsin, A and B, are found in equal amounts in cattle pancreas. They are very similar proteins (80% identical), but have significantly different proteolytic characteristics (Hartley 1964, Meloun et al. 1966, Smillie et al. 1968, and Gráf et al. 2004).

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.

Chymotrypsin, Alpha, 3x cryst., TLCK treated – CDTLCK is 3X 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.

• SUPPLIER:

  Worthington Biochemical

• STATUS:

  In Stock

• SIZE:

  25 mg