Hydrolysis of dipeptides by human and ovine placentas.

Abstract:

:Human and ovine placental tissue homogenates were assayed for dipeptidase activity in vitro. Glycyl-L-leucine, L-leucyl glycine, glycyl-L-lysine, and L-lysyl glycine were hydrolyzed by placental homogenates. The pH optimum for the reaction was 8.0. The relationship between enzyme activity and concentration was linear for placental homogenate concentrations between 0.01 and 0.10 mg protein/ml of reaction mixture. Enzyme activities were 1.92 +/- 0.12 (S.E.) micromoles/min/mg protein for hydrolysis of glycyl-L-leucine, 0.34 +/- 0.06 (S.E.) micromoles/min/mg protein for hydrolysis of glycyl-L-lysine by human placenta, and 2.79 +/- 0.80 micromoles/min/mg protein and 0.41 +/- 0.25 micromoles/min/mg protein, respectively, by ovine placenta. The infusion of glycyl-L-leucine into the uterine artery of unstressed catheterized pregnant ewes yielded increased concentrations of both component amino acids in uterine venous blood and of leucine in umbilical venous blood.

journal_name

Pediatr Res

journal_title

Pediatric research

authors

Crandell SS,Adcock EW 3rd,Morriss FH Jr

doi

10.1203/00006450-198104000-00013

subject

Has Abstract

pub_date

1981-04-01 00:00:00

pages

357-61

issue

4 Pt 1

eissn

0031-3998

issn

1530-0447

journal_volume

15

pub_type

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