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Article
October 1961

Purification of Hyaluronidase from Bovine Testes

Author Affiliations

Los Angeles
Department of Surgery, Division of Ophthalmology, and the Department of Physiological Chemistry, University of California Medical Center, Los Angeles.

Arch Ophthalmol. 1961;66(4):534-538. doi:10.1001/archopht.1961.00960010536016
Abstract

Introduction  The potential value of hyaluronidase as an agent for enzymatic degradation of hyaluronic acid in the eye has led to efforts to purify and characterize this substance. The various techniques of protein purification that have been applied to the preparation of hyaluronidase from bovine testes include: (a) ammonium sulfate precipitation,1,2 (b) fractionation in aqueous solution with salts of heavy metals, viz., CuSO4 and Pb(OAc)2,2 (c) electrophoresis in free solution,2 (d) cold ethanol fractionation,3 and (e) chromatography on the cation exchange resin, IRC-50.4,5It appeared to us that the application of a few additional techniques now available might permit one to obtain an enzyme preparation of considerably higher specific activity than any hitherto available. Some of the methods listed would then serve for the initial stages of the purification process.A preliminary investigation in this laboratory showed that methods (a) and (b) would

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