Enzymes for Research
The chymotrypsins, of which there are several, are serine proteases derived from the inactive precursor Chymotrypsinogen-A (Alpha– Chymotrypsinogen) and B, which are present in the pancreas and pancreatic juice. Chymotrypsinogen-A is activated by Trypsin, and depending on the method of activation, the principle chymotrypsins may be obtained.
These are referred to as Alpha, beta, gamma, delta and pi chymotrypsins.
Chymotrypsin specificity: hydrolysis of peptide bonds formed by hydrophobic amino acid residues such as Tyrosine, Phenylalanine and Tryptophan. It hydrolases tyrosyl, tryptophanyl, phenylalanyl
peptides, amides and esters. Slow hydrolysis also occurs with aspartate, glutamine, histidine, leucine, lysine, methionine, serine and threonine.
Trypsin is widely distributed in animals and in some bacteria and is classed as a serine protease. Trypsin is present in the pancreas and pancreatic juice in vertebrates. Trypsinogen, secreted into the duodenum as a pro-enzyme, is activated by Enterokinase secreted by the duodenal mucosa. Trypsin is obtained by activation of its inactive precursor (Trypsinogen) by Enterokinase and by Trypsin itself. Calcium stimulates the autoactivation of Trypsinogen.
Trypsin has a high degree of substrate specificity as it catalyses the hydrolysis of peptide bonds on the carboxyl terminus of positively charged amino acids such as Lysine and Arginine. Trypsin has a weak action on native proteins and will not hydrolyze serum globulins, haemoglobin, ovalbumin or collagen.
Testicular hyaluronidase is a typical glucosidase having both endohexosaminidase and transglycosidase activity.
Substrates are hyaluronic acid and also chondroitin sulphate A and C. Products of hydrolysis are a series of oligosaccharides, mainly tetrasaccharides. Hyaluronidase is often used in conjunction with collagenase to
dissociate the extracellular matrix between cells of animal tissue, in order to release viable cells for use in tissue culture. It may also be used to clarify synovial fluids in order to make cell counts possible.
Trypsin and Chymotrypsin are proteolytic pancreatic enzymes which are secreted as inactive precursors Trypsinogen and Chymotrypsinogen. Trypsin and Chymotrypsin are obtained by the activation of these
precursors. Their catalytic function is to hydrolyse the peptide bonds of proteins. BBI’s Trypsin/Chymotrypsin is extracted from Bovine Pancreas. It is available in 6:1 and 1:1 ratios.
Deoxyribonuclease (DNase) occurs predominantly in the pancreas, but has also been found in other tissues and in the salivary glands. DNase is an endonuclease enzyme that hydrolyses phosphodiester
bonds adjacent to pyrimidine nucleotides of deoxyribonucleic acid (DNA), yielding 5’-phosphate terminated polynucleotides with a free hydroxyl group at the 3’ position.