|Molecular Biology||Storage: -20°CShipping: Blue Ice|
Hyaluronidase catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido-2-deoxy-beta-D-glucose and D-glucose residues in hyaluronate. Hyaluronate 4-glycanohydrolase (EC 18.104.22.168) catalyzes the depolymerization of mucopolysaccharides, hyaluronic acid, and the chondroitin sulfates A and C. The enzyme is widely distributed in animal tissues but is found in great concentrations in the bovine and ovine testes. It is also produced by a number of bacteria. Hyaluronidase from bovine testes has a molecular weight of 55,000. Purified hyaluronidase is used clinically for the intradermal administration of large volumes of fluid when intravenous injections are contraindicated. The enzyme is administered prior to or simultaneously with the fluid and it facilitates absorption of the fluid.
Soluble in ddH2O or dilute buffer.
That amount of enzyme which liberates one micromole of N-acetylglucosamine per minute at 37°C and pH 4.0. The assay is based on the following reaction:
Hyaluronic acid ------> Acetylglucosamine
An anhydro sugar is first formed from N-acetylglucosamine, followed by the conversion of the sugar into its furan derivative, as a result of increasing the acidity of the solution. This furan derivative then reacts with p-dimethylamino-benzaldehyde to form a colored complex, which is measured spectrophotometrically at 585nm.
Storage and Stability:
Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile buffer or ddH2O. Aliquot and store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Supplied as a dialyzed, lyophilized powder.
Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Human Biochemistry; Orten, J.M., and Neuhaus, O.W.; 10th edition, Pg. 411, 1982. Mosby, St. Louis
Methods of Enzymatic Analysis, Bergmeyer, H.U., ed., Vol. 2, pp. 944-948, Academic Press, New York, 1974