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Development of tyrosine aminotransferase and para-hydroxyphenylpyruvate dioxygenase activities in fetal and neonatal human liver.
J J Ohisalo, … , T Laskowska-Klita, S M Andersson
J J Ohisalo, … , T Laskowska-Klita, S M Andersson
Published July 1, 1982
Citation Information: J Clin Invest. 1982;70(1):198-200. https://doi.org/10.1172/JCI110593.
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Research Article

Development of tyrosine aminotransferase and para-hydroxyphenylpyruvate dioxygenase activities in fetal and neonatal human liver.

Abstract

In livers of fetuses of 220--340 g body wt, total cytosolic tyrosine aminotransferase activity was 1.0 nmol of product/mg of protein per min, and the corresponding values for autopsy livers of newborns of 740--1,475 g and 2,600--3,650 g were 1.5 and 5.7, respectively, as compared with the adult value of 12.7. On the other hand, para-hydroxyphenylpyruvate dioxygenase activity is at adult level already in fetuses less than 340 g body wt. The Km value for tyrosine of tyrosine aminotransferase (1 mM) was considerably higher than the corresponding value for para-hydroxyphenylpyruvate of para-hydroxyphenylpyruvate dioxygenase (50 micro M). These results suggest that tyrosine aminotransferase is the rate limiting enzyme in the catabolism of tyrosine in premature infants.

Authors

J J Ohisalo, T Laskowska-Klita, S M Andersson

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