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Phenylalanine hydroxylase ofMacaca irus. Purification of two components of the enzyme

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Enzymology
0005-2744
Publisher
Elsevier
Publication Date
Volume
235
Issue
1
Identifiers
DOI: 10.1016/0005-2744(71)90033-7
Disciplines
  • Biology

Abstract

Abstract 1. 1. Phenylalanine hydroxylase ( l-phenylalanine, tetrahydropteridine: O 2 oxidoreductase (4-hydroxylating), EC 1.14.3.1) has been purified up to 424-fold from the liver of the Cynomolgus monkey ( Macaca irus). This was achieved after stabilization of the enzyme during extraction and chromatography. 2. 2. In the final stages of purification two fractions have been separated, both of which are essential for full activity. 3. 3. Conditions for maximal activity have been established and preliminary kinetic studies have been performed. The optimum pH was found to be 7.6. The K m for l-phenylalanine was found to be 5.7·10 −4 M and 8.5·10 −5 M for 2-amino-6,7-dimethyl-4-hydroxy-5,6,7,8-tetrahydropteridine hydrochloride.

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