Identification, characterization, and partial purification of mammalian skin wound hyaluronidase

Charles Bertolami, R. B. Donoff

Research output: Contribution to journalArticle

Abstract

A recently described mammalian wound hyaluronidase is successfully characterized and partially purified in the current study. Peak enzyme activity occurred on postwound day 7, pH optimum 4.5. Both crude and purified would enzyme exhibited endoglycosidic activity against hyaluronate and chondroitin-4-sulfate but not against chondroitin-6-sulfate or dermatan sulfate. A 5.3 fold increase in activity was obtained by the DEAE-Sephadex purification technique described. Polyacrylamide gel electrophoresis yielded a single major band near the gel's midrange and one minor band of less electrophoretic mobility. These enzyme characteristics support a biochemical analogy between tissue repair in skin and numerous developmental systems and may provide a simple means for enzymatic differentiation among chondroitin sulfate isomers.

Original languageEnglish (US)
Pages (from-to)417-421
Number of pages5
JournalJournal of Investigative Dermatology
Volume79
Issue number6
StatePublished - 1982

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Hyaluronoglucosaminidase
Chondroitin Sulfates
Purification
Skin
Wounds and Injuries
Enzymes
Dermatan Sulfate
DEAE-Dextran
Electrophoretic mobility
Enzyme activity
Electrophoresis
Isomers
Polyacrylamide Gel Electrophoresis
Repair
Gels
Tissue

ASJC Scopus subject areas

  • Dermatology

Cite this

Identification, characterization, and partial purification of mammalian skin wound hyaluronidase. / Bertolami, Charles; Donoff, R. B.

In: Journal of Investigative Dermatology, Vol. 79, No. 6, 1982, p. 417-421.

Research output: Contribution to journalArticle

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