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38594 Hyaluronidase, Ovine Testes

Hyaluronidase, Ovine Testes MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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      Overview

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      Native hyaluronidase from ovine testes. Hyaluronic acid degrading endoglycosidase that catalyzes the hydrolysis of 1,4 linkages in chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate esters, and hyaluronic acid.
      Note: 1 KU = 1000 units.
      Catalogue Number38594
      Brand Family Calbiochem®
      References
      ReferencesLokeshwar, V.B., et al. 2002. J. Biol. Chem. 277, 33654.
      Borders, C.L., and Raftery, M.A. 1968. J. Biol. Chem. 243, 3756.
      DeSalequi, M., et al. 1967. Arch. Biochem. Biophys. 121, 548.
      Lowry, O.H., et al. 1951. J. Biol. Chem. 193, 265.
      Product Information
      CAS number37326-33-3
      Unit of DefinitionOne unit is defined as the amount of enzyme that will cause the same turbidity reduction as 1.0 unit of International Standard preparation.
      EC number3.2.1.35
      FormWhite lyophilized solid
      Quality LevelMQ100
      Applications
      Biological Information
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 5 days at 4°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalog Number GTIN
      38594 0

      Documentation

      Hyaluronidase, Ovine Testes SDS

      Title

      Safety Data Sheet (SDS) 

      Hyaluronidase, Ovine Testes Certificates of Analysis

      TitleLot Number
      38594

      References

      Reference overview
      Lokeshwar, V.B., et al. 2002. J. Biol. Chem. 277, 33654.
      Borders, C.L., and Raftery, M.A. 1968. J. Biol. Chem. 243, 3756.
      DeSalequi, M., et al. 1967. Arch. Biochem. Biophys. 121, 548.
      Lowry, O.H., et al. 1951. J. Biol. Chem. 193, 265.
      Data Sheet

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision26-Febuary-2009 RFH
      DescriptionNative hyaluronidase from ovine testes. Catalyzes the hydrolysis of 1,4 linkages between N-acetylhexosamine and D-glucuronate residues in chondroitin, chondroitin-4-sulfate, chrondroitin-6-sulfate esters, and hyaluronic acid. Has an optimal pH of 4.5-6.0. Hydrolyzes the endo-N-acetyl-hexosaminic bonds of hyaluronic acid and chondroitin sulfate A and C to yield tetrasaccharide residues. Hyaluronidase activity is inhibited by the presence of Fe2+, Fe3+, Cu2+, and Mn2+.
      FormWhite lyophilized solid
      Recommended reaction conditions
      Assay Protocol Principle of Assay: Hyaluronic acid is measured by its ability to yield turbidity with an acidic albumin solution. The turbidity produced is a function of hyaluronic acid concentration and hence can be related to the activity of the enzyme. Reagents: • 1N NaOH • 0.3 M Sodium Phosphate Buffer, pH 5.3-5.35 • Hyaluronic Acid Solution (0.2 mg/ml in 0.3 M sodium phosphate buffer, pH 5.3-5.35). May heat in a boiling water bath for a few minutes to dissolve. Alternatively, place at 4°C overnight. Stir for about 1 h on the next day to dissolve completely. • Enzyme Diluent (0.02 M sodium phosphate buffer, pH 6.9, containing 0.45% NaCl and 0.01% BSA) • 5N Hydrochloric Acid • Acid Albumin Solution (10 mg of BSA, Fraction V, in 10 ml of 0.5 M sodium acetate buffer, pH 4.2). Adjust pH to 3.75 with few drops of 50 mM HCl. This solution is stable for 2 days at 4°C. • Standard Hyaluronidase Solution (10 I.U./ml). • Enzyme solution: Dissolve 10 mg of Hyaluronidase in 2 ml of ice-cold enzyme diluent (see above). Dilute to 2.0 I.U./ml just prior to use. Test Procedure: (Incubation temperature: 38°C; Wavelength; 600 nm; d = 1 cm) Preparation of Standard curve: Into a series of test tubes add reagents, as follows:

      Table 1: Preparation of Standard Curve

      1. Thoroughly mix and place the tubes at 38°C for 5 min. 2. At time zero add 1 ml of hyaluronic acid solution to each tube (for convenience allow 30 s intervals between each tube). Mix, stopper and incubate at 38°C for exactly 45 min. 3. Then add 10 ml of acid albumin solution to each tube and mix rapidly by inversion. Allow to stand for 5 min at room temperature. Read absorbance at 600 nm against a blank. 4. Construct a standard curve by plotting absorbance against the I.U./ml. Measurement of Hyaluronidase Activity: Pipette 1 ml of each diluted sample into test tubes at 38°C and repeat steps 1 to 4 (see above). Obtain hyaluronidase concentration (I.U./ml) for each sample solution using the standard curve.

      Figure 1: Calculations

      Protein Determination: Protein Content can be determined by Lowry's method.
      CAS number37326-33-3
      EC number3.2.1.35
      Unit definitionOne unit is defined as the amount of enzyme that will cause the same turbidity reduction as 1.0 unit of International Standard preparation.
      SolubilityReconstitute at 5 mg/ml in 20 mM sodium phosphate, 0.45% NaCl, and 0.01% BSA, pH 6.9. At a concentration of 5 mg/ml the solution will be clear and colorless.
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, store in the refrigerator (4°C). Stock solutions are stable for up to 5 days at 4°C.
      Toxicity Standard Handling
      Merck USA index14, 4758
      ReferencesLokeshwar, V.B., et al. 2002. J. Biol. Chem. 277, 33654.
      Borders, C.L., and Raftery, M.A. 1968. J. Biol. Chem. 243, 3756.
      DeSalequi, M., et al. 1967. Arch. Biochem. Biophys. 121, 548.
      Lowry, O.H., et al. 1951. J. Biol. Chem. 193, 265.