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PMID: 6123525 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Journal of clinical investigation ·Vol. 70 ·No. 1 ·1982-07-00 ·Pages 198-200

Ohisalo JJ, Laskowska-Klita T, Andersson SM

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.

MeSH Terms
4-Hydroxyphenylpyruvate Dioxygenase/metabolism Adult Body Weight Female Fetus/enzymology Humans Infant, Newborn Liver/enzymology Oxygenases/metabolism Pregnancy Tyrosine Transaminase/metabolism
Chemicals
Oxygenases 4-Hydroxyphenylpyruvate Dioxygenase Tyrosine Transaminase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ohisalo J J
Laskowska-Klita T
Andersson S M
References (15)
15 references, click to expand
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Article Info
Journal
The Journal of clinical investigation
Abbr.
J Clin Invest
ISSN
0021-9738
Published
1982-07-00
Pages
198-200
Language
English
Region
United States
NLM ID
7802877
PMCID
PMC370242
Subset
IM
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