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Tryptophan Hydroxylase in Nucleated Thrombocytes of the Domestic Fowl.

Authors :
Sorimachi, Masaru
Kataoka, Kiyoshi
Hori, Seiki
Hori, Shinichiro
Fujisawa, Hitoshi
Source :
European Journal of Biochemistry; 1973, Vol. 33 Issue 3, p486-493, 8p
Publication Year :
1973

Abstract

Using the labeled CO<subscript>2</subscript> trapping method, tryptophan hydroxylase activity was detected in the nucleated thrombocytes of the domestic fowl, but not in the mammalian platelets. This enzyme activity was around a 5-hydroxytryptophan production of 60 pmol×mg protein<superscript>-1</superscript>××h<superscript>-1</superscript>. Certain properties such as optimal pH (7.0), K<subscript>m</subscript> value (12 μM), requirement for cofactor (2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydroptetidine) and inhibition by p-chlorophenylalanine indicated a close resemblance to tryptophan hydroxylase from brain tissue. Solubilization of this enzyme was to some extent successful by digitonin treatment of the cells. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
33
Issue :
3
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
13599400
Full Text :
https://doi.org/10.1111/j.1432-1033.1973.tb02707.x