Technical Data
H7981
Hyaluronidase, Bovine, Highly Purified
5000U
15KU
Molecular Biology Storage: -20CShipping: 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 3.2.1.35) 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.

Activity (USP/NF units/mg dw):
3000u/mg

Absorbance (A280@mg/ml):
As Reported

Unit Definition:
One unit is based on the change in absorbency (turbidity) at 540nm of an internal standard.

Quality Control:
SDS-PAGE

Storage and Stability:
Lyophilized powder may be stored at -20C. Stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Prepare fresh before use.

Certificate of Origin:
The raw animal product (bovine glands, organs and tissue) used in the manufacturing of Hyaluronidase is derived from materials of USDA-approved origin. It was collected in USDA or equivalent approved facilities and inspected to be free of disease.

CAS Number:
37326-33-3
Source: Bovine testes
Purity: Chromatographically purified
Form: 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.
1. Human Biochemistry; Orten, J.M., and Neuhaus, O.W.; 10th edition, Pg. 411, 1982. Mosby, St. Louis. 2. Methods of Enzymatic Analysis, Bergmeyer, H.U., ed., Vol. 2, pp. 944-948, Academic Press, New York, 1974. 3. Borders, C., and Raftery, M.. J Biol Chem 243, 3756, 1968. 4. Khorlin, A., Vikha, I., and Milishnikov, A.. F.E.B.S. Lett. 31, 107, 1973. 5. DeSalequi, M., Plonska, H., and Pigman, W. Arch Biochem Biophys 121, 548, 1967. 6. Warren, G., Seifter, J., and Glassman, J. Nature 194, 770, 1962. 7. Ludowieg, J., Vennesland, B., and Dorfman, A. J Biol Chem 236, 333, 1961. 8. Rappaport, M., Meyer, K., and Linker, A. J Am Chem Soc 73, 2416, 1951. 9. Yang, C., and Srivastav, P. J Biol Chem 250, 79, 1975.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.