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/lp/wiley/purification-and-characterization-of-the-tyrosinase-isozymes-of-pine-g1msNFwWs0
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- Publisher
- Wiley Subscription Services, Inc., A Wiley Company
- Copyright
- Copyright © 1998 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1521-6543
- eISSN
- 1521-6551
- DOI
- 10.1080/15216549800203122
- Publisher site
- See Article on Publisher Site
Abstract
Three tyrosinase isozymes were purified to electrophoretic homogeneity from pine needles. The molecular weight of the three isozymes (P1, P2 and P3) were approximately 65000, 50000 and 45000, and the pI values were 6.2, 5.9 and 5.3, respectively. The three isozymes have a number of common properties. These include amino acid composition, substrate specificity, response to inhibition. The amino acid compositions of the three isozymes showed the characteristic high contents of glycine, serine and glutamic acid residues. The three isozymes exhibited high substrate specificity towards pyrogallol. The Km values of the three isozymes for L‐DOPA ranged from 8.7 to 10 raM. L‐ascorbic acid and β‐mercaptoethanol, glutathione and sodium diethyldithiocarbamate notably inhibited the enzymatic activities.
Journal
IUBMB Life – Wiley
Published: Jul 1, 1998
Keywords: ; ;