Enzymes accelerate, or catalyse, chemical reactions, and they are known to catalyse more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.

Tritirachium album proteinase K, MP Biomedicals

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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) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0,1 to 0,5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

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Neuraminidase, MP Biomedicals

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Neuraminidase (Sialidase: Acylneuraminyl hydrolase; EC 3.2.1.18) From Arthrobacter ureafaciens lyophilised powder with salts. The salts are composed of sodium-potassium phosphate to give a solution of 10 mM phosphate buffer (pH 7) when enzyme is reconstituted with water to make activity of 1 unit per ml. Activity: >60 units/mg protein for NAN-lactose >25 units/mg protein for bovine submaxillary mucin >20 units/mg protein for colominic acid Protein is determined by the method of Lowry et al. with bovine albumin as a standard.6 Unit definition: One unit will liberate 1,0 µmole of N-acetyl-neuraminic acid (NANA) per minute at pH 5,0 at 37 °C, using either one NAN-lactose, bovine submaxillary mucin, or colominic acid as a substrate.

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Bovine deoxyribonuclease I (from Pancreas), MP Biomedicals

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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 average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin.

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beta-Galactosidase, MP Biomedicals

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Inhibitors: p-Chloromercuribenzoate, lodoacetamide, heavy metal ions (Zn²⁺, Fe²⁺, Zn²⁺, Cd²⁺, Cu²⁺, Pb²⁺, Ag⁺, Hg²⁺), Ionic Detergents (SDS, DAC, etc.). Contaminants: The preparation is practically free from other glycosidases (a-galactosidase, a-,b-glucosidase, a-,b-mannosidase, etc.) and proteinase. Principle: o-Nitrophenyl-b-D-galactopyranoside (ONPG) b-galactosidase > o-Nitrophenol (ONP) +D-Galactose. The appearance of o-nitrophenol is measured at 410 nm by spectrophotemetry. Thermal stability: below 50 °C (pH 7,3; 15 min) (Lit.), Optimum Temperature: 50 to 55 °C (Lit.).

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Papain, MP Biomedicals

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Activators: Papain is activated by cysteine, sulphide, sulphite and more. It is enhanced when heavy metal binding agents such as EDTA are also present. N-bromosuccinimide enhances the activity. Inhibitors: Substances which react with sulphydryl groups including heavy metals, carbonyl reagents. Aldehydes are papain inhibitors. Benzoylamidoacetonitrile is an inhibitor. See Shapira and Arnon (1967a and b) on antibody inhibitors. Papain may be inactivated by H₂O₂ generated by γ-irradiation of H₂O⁻ the active SH group being oxidised to sulphenic acid. Specific inhibitors are AEBSF, antipain, cystatin, E-64, leupeptin, PMSF, TLCK and TPCK.

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Elastase, MP Biomedicals

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Elastase is prepared from porcine pancreas. It is lyophilised and water soluble. Elastase is chromatographically prepared by the method of Narayanan and Anwar. In the method, 2 times crystalline elastase is adsorbed on a column of DEAE-Sephadex A50 to separate elastase and non-specific protein components. The elastase component is further purified by chromatography on a column of CM-Cellulose using a sodium chloride gradient to elute the elastase. The latter is dialysed until chloride-free and then lyophilised. During its preparation the elastase is held below a pH of 5,5 for greater than 24 hours. Two times crystallised from the euglobin fraction of porcine pancreas by the method of Lewis et al. Does not contain trypsin or chymotrypsin.

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Bovine alpha-Chymotripsin (Pankreas)

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Preparation Method Produced from 3× crystallised chymotrypsinogen α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology. Chymotrypsin preferentially catalyses 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. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.

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Aldolase, MP Biomedicals

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Aldolase is a tetrameric protein. It catalyses a key reaction in glycolysis and energy production:D-Fructose 1,6-bisphosphate aldolase → dihydroxyacetone phosphate + D-glyceraldehyde-3-phosphate. Aldolase is present in all animal tissue and in most microorganisms. There are two classes of aldolases. Class I aldolase is found in animal and higher plant tissue. Class II aldolase is found in primitrive cells such as yeasts and bacteria. Class I aldolase is characterised by not requiring a bivalent metal cofactor and the formation of a ketimine Schiff base intermediate with the substrate dihydroxyacetone phosphate. Class II aldolase requires a metal cofactor and is inhibited by EDTA. Three types of aldolase exist in animal tissue. The major form, type A is found in muscle; type B is found in liver tissue and type C (plus some type A) is found in brain tissue. Aldolase forms five isozymes which may to various degrees be organ specific.