Details

Autor(en) / Beteiligte

• Wilson, D. Wright
• Wilson, Helene C

Titel

Digestion of purine ribonucleotides by intestinal enzymes of the developing rat fetus

Ist Teil von

• The American journal of physiology, 1965-12, Vol.209 (6), p.1155-1158

Ort / Verlag

United States

Erscheinungsjahr

1965

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 1 Department of Biochemistry, University of Pennsylvania Medical School, Philadelphia, Pennsylvania Small segments of intestine from fetal rats were incubated in the presence of guanosine monophosphate (GMP) or adenosine monophosphate (AMP) and the products of hydrolysis identified by paper chromatography. All of the enzymes required to decompose GMP and AMP to uric acid and allantoin that were found in the adult intestine were also found in the 19-day fetal intestine. These were: nucleotide phosphatase, adenosine deaminase, guanosine-inosine phosphorylase, guanase, xanthine oxidase, and presumably uricase. The 16-day fetal intestine lacked xanthine oxidase, at least in sufficient amount to give ultraviolet spots on the chromatograms, for xanthine and uric acid. In one experiment on a 15-day fetus, inosine phosphorylase was also lacking, and one on a 13-day fetus gave positive evidence of only nucleotide phosphatase. It is inferred that there is a gradual development of these enzymes in the fetal life of the rat, the ones decomposing the more complex molecules of the nucleotides and the nucleosides appearing earlier than those decomposing the bases. There are, however, no data from these experiments to indicate how early uricase is formed, since uric acid was not found among the decomposition products of GMP or AMP digestion until the 19th day. Key Words: development of intestinal enzymes Submitted on March 3, 1965