The most recently published method for the assay of testicular hyaluronidase preparations was based on the premise that the enzyme also exhibited carboxylesterase activity towards indoxyl acetate. Studies on the relative enzyme activities of various hyaluronidase preparations towards hyaluronate and indoxyl acetate, the relative stabilities towards pH, temperature and mechanical shaking and the behaviour towards a variety of inhibitors, showed that the activities towards the two substrates reflected the presence of at least two different enzyme systems in the preparations. Gel chromatography and polyacrylamide-gel-electrophoresis experiments confirmed these conclusions and the collective findings clearly establish that methods based on the use of indoxyl acetate cannot be employed to measure testicular hyaluronidase activity.
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May 1971
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Research Article|
May 01 1971
Unsuitability of indoxyl acetate as a substrate for the assay of testicular hyaluronidase
C. Rhodes;
C. Rhodes
1Biorex Laboratories Ltd., Biorex House, London N1 2HB, U.K.
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K. S. Dodgson;
K. S. Dodgson
2Department of Biochemistry, University College, Cathays Park, Cardiff CF1 1XL, U.K.
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A. H. Olavesen;
A. H. Olavesen
2Department of Biochemistry, University College, Cathays Park, Cardiff CF1 1XL, U.K.
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B. Högberg
B. Högberg
3AB Leo, Halsingborg, Sweden
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Publisher: Portland Press Ltd
© 1971 The Biochemical Society
1971
Biochem J (1971) 122 (4): 575–582.
Citation
C. Rhodes, K. S. Dodgson, A. H. Olavesen, B. Högberg; Unsuitability of indoxyl acetate as a substrate for the assay of testicular hyaluronidase. Biochem J 1 May 1971; 122 (4): 575–582. doi: https://doi.org/10.1042/bj1220575
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