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PMID: 4219137 Published · ppublish English Journal Article

The amine oxidases of human placenta and pregnancy plasma.

The Biochemical journal ·Vol. 139 ·No. 1 ·1974-04-00 ·Pages 169-81

Bradsley WG, Crabbe MJ, Scott IV

Abstract

1. The purification of monoamine oxidase and diamine oxidase from normal human term placental tissue is described. 2. The properties of these enzymes are reported and compared with the properties of unpurified human pregnancy plasma. 3. This comparison shows that the amine oxidase of pregnancy plasma has properties corresponding to purified placental diamine oxidase, suggesting a placental origin for the plasma enzyme system. 4. Detailed kinetic study of the purified placental diamine oxidase suggests that it has a Ping Pong sequence, a mechanism of action and rate-limiting step similar to the diamine oxidase of pig kidney. 5. It is suggested that the enzyme system is important in protecting the foeto-placental unit from excesses of biogenic amines.

MeSH Terms
Amine Oxidase (Copper-Containing)/blood,isolation & purification,metabolism Chromatography, Gel Chromatography, Ion Exchange Female Humans Kinetics Mathematics Monoamine Oxidase/blood,isolation & purification,metabolism Phenanthrolines/pharmacology Placenta/enzymology Pregnancy Structure-Activity Relationship Time Factors
Chemicals
Phenanthrolines Amine Oxidase (Copper-Containing) Monoamine Oxidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bradsley W G
Crabbe M J
Scott I V
References (13)
13 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1974-04-00
Pages
169-81
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1166264
Subset
IM
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