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Hyaluronidase isolated from the lysosomes of rat liver (1) was purified 1300-fold by ammonium sulfate precipitation, chromatography on hydroxylapatite, and chromatography on Sephadex G-100. The most purified fraction gave two peaks on sedimentation in the ultracentrifuge, the faster of the two being yellow and possessing no enzymic activity. The slower peak showed a single band on acrylamide gel electrophoresis. The molecular weight of the enzyme was calculated to be 89,000 based on sedimentation equilibrium data.
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Aronson et al. (1967) studied this question.
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