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Purification and characterization of the tyrosinase isozymes of pine needles
Author(s) -
Kong KwangHoon,
Lee JongLiong,
Park HeeJoong,
Cho SungHye
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203122
Subject(s) - tyrosinase , isozyme , characterization (materials science) , chemistry , biochemistry , botany , enzyme , biology , nanotechnology , materials science
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.