Elastase is an enzyme from the class of proteases (peptidases) that break down proteins. It hydrolyzes peptide bonds, especially those adjacent to neutral amino acids. Hydrolyses elastin Digests hemoglobin, casein, and fibrin One unit will solublize 1 mg of elastin in 20 minutes at…

Trypsin consists of a single chain polypeptide of 223 amino acid residues. Member of the serine protease family Dissolves blood clots in its microbial form Treats inflammation in its pancreatic form Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues.…

Collagenase is a protease which cleaves the triple-helical protein called collagen. There are three types of tissue collagenases, and these belong to the matrix metalloproteinases (MMP) family. Collagenase from Clostridium histolyticum has extensive use in biological studies, where it is used to…

Acetyl-CoA is produced via beta-oxidation of fatty acids, via the metabolism of carbohydrates - glucose 6-phosphate to pyruvate to acetyl-CoA and via the catabolism of amino acids. Acetyl-CoA has a number of metabolic opportunities. It is metabolized in the tricarboxylic acid cycle to produce…

Biliverdin Dihydrochloride is a bile pigment component. An oxidized metabolite of bilirubin caused when bilirubin reacts with reactive oxygen species. Biliverdin IX is composed of alpha, beta, gamma and delta isomers. Biliverdin dihydrochloride was found responsible for cytoprotection. It was…

Collagenases degrade native helical collagen fibrils. It has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. Collagenase is used for tissue dissociation combined with other enzymes such as elastase, trypsin,…

Papain is a sulfhydryl protease from Carica papaya latex. Cleaves peptide bonds of basic amino acids, leucine, or glycine Hydrolyzes esters and amides One unit will hydrolyze 1.0 µmole of N-alpha-benzoyl-L-arginine ethyl ester (BAEE) per minute at 25°C and pH 6.2 Papain…

Collagenases degrade native helical collagen fibrils. Plays an important role in connective tissue metabolism Produced by specific cells involved in repairs and remodeling processes Type II enzyme that contains greater clostripain activity Collagenase is used for collagen…

Hyaluronidase is a glycoprotein containing 5% mannose and 2.17% glucosamine, it catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- β-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a…

Hyaluronidase is a glycoprotein containing 5% mannose and 2.17% glucosamine, it catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- b-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a…

A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond. Produced from 3x Crystallized chymotrypsinogen Used to treat pancreatic insufficiency Used in traumatology Chymotrypsin…

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The…

Ribonuclease A, and to a greater extent its oligomers and some homologs (such as onconase from frogs), have cytotoxic and cytostatic effects, particularly on cancer cells.This attribute has led to the development of onconase as a cancer therapeutic. Ribonuclease A is used to remove RNA from DNA…

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles)…

Diamide is used as a thiol oxidizing agent. It has also been used to titrate protein glutathiolation to discriminate from other oxidative protein modifications. Diamide treatment increased protein glutathiolation in a concentration-dependent manner and had comparably little effect on…

L-glutamic dehydrogenase is a pyridine nucelotide enzyme which catalyzes the reversible oxidative deamination of L-glutamate to α-keto-glutarate and ammonia. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway…

Naphthol AS-D chloroacetate is a substrate for histochemical localization of esterases.

Roseoflavin is a weak antibacterial agent active against some gram-positive bacteria, especially Staphylococcus aureus, Sarcina latea, Bacillus cereus and Bacillus subtilis. Also exhibits antiriboflavin activity and inhibits the biosynthesis of riboflavin by a repressor mechanism.

Trypsin inhibitor from soybeans is a monomeric protein containing 181 amino acid residues in a single polypeptide chain crosslinked by two disulfide bridges. Reversible serine protease inhibitor Inhibits factor Xa, trypsin, chymotrypsin, kallikrein and plasmin One unit will inhibit…

A highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber, suitable for both protein and nucleic acid isolation, it exhibits proteolytic…