Hofinger, Edith S. A. and Bernhardt, Guenther and Buschauer, Armin (2007) Kinetics of Hyal-1 and PH-20 hyaluronidases: Comparison of minimal substrates and analysis of the transglycosylation reaction. GLYCOBIOLOGY, 17 (9). pp. 963-971. ISSN 0959-6658, 1460-2423
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The availability of recombinant expression systems for the production of purified human hyaluronidases PH-20 and Hyal-1 facilitated the first detailed analysis of the enzymatic reaction products. The human recombinant enzymes, both expressed by Drosophila Schneider-2 (DS-2) cells, were compared to bovine testicular hyaluronidase (BTH), a commercially available hyaluronidase preparation, which has long been considered a prototype of mammalian hyaluronidases. The conversion of low molecular weight hyaluronic acid ( HA) fragments was detected by a capillary zone electrophoresis (CZE) method. Surprisingly, the HA hexasaccharide, which is generally accepted to be the minimum substrate of BTH, was not a substrate of recombinant human PH-20 and Hyal-1. However, HA octasaccharide was converted efficiently by both enzymes, thus representing the minimum substrate for human PH-20 and Hyal-1. Additionally, BTH was shown to catabolize the HA hexasaccharide at pH 4.0 mainly by hydrolysis, while at pH 6.0 transglycosylation prevailed. Human PH-20 was found to catalyze both hydrolysis and transglycosylation of the HA octasaccharide. On the contrary, human Hyal-1 converted the HA octasaccharide mainly by hydrolysis with transglycosylation products occurring only at high substrate concentrations (>= 500 mu M). The differences between the hyaluronidase subtypes and isoenzymes were much more prominent than expected. Obviously, the different hyaluronidase subtypes have evolved into very specialized enzymes with respect to their catalytic mechanism of action.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BOVINE TESTICULAR HYALURONIDASE; CAPILLARY-ELECTROPHORESIS; IONIC-STRENGTH; MORGAN-ELSON; HUMAN SERUM; PURIFICATION; HYDROLYSIS; PROTEIN; ENZYME; ACID; capillary electrophoresis; Drosophila Schneider-2; cells; Hyal-1; PH-20; transglycosylation |
| Subjects: | 600 Technology > 615 Pharmacy |
| Divisions: | Chemistry and Pharmacy > Institute of Pharmacy > Alumni or Retired Professors > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Dec 2020 12:11 |
| Last Modified: | 01 Dec 2020 12:11 |
| URI: | https://pred.uni-regensburg.de/id/eprint/32282 |
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