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SAMUEL M. MOZERSKY, Ph.D.; BRADLEY R. STRAATSMA, M.D.; JOHN M. STEFFY, B.A.; ANN McFARLIN, B.A.

Arch Ophthalmol. 1961;66(4):534-538.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

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.^4,5

It 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 . . . [Full Text PDF of this Article]

Author Affiliations
Los Angeles

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

Footnotes
Submitted for publication May 12, 1961.

This investigation was supported by grants-in-aid from (1) the Doheny Eye Foundation, (2) the Knights Templar Eye Foundation, Inc., and (3) the U.S. Public Health Service, No. B-2327.

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