Back to Search
Start Over
Human placenta cytidine deaminase: a zinc metalloprotein.
- Source :
-
Biochemistry and molecular biology international [Biochem Mol Biol Int] 1997 Jul; Vol. 42 (3), pp. 469-76. - Publication Year :
- 1997
-
Abstract
- Cytidine deaminase, a tetrameric enzyme purified from human placenta, was shown to contain a single atom of tightly bound zinc per subunit by Inductively Coupled Plasma Optical Emission Spectrometry analysis. The metal appears to be involved in catalysis, as suggested by the inhibition exerted by 1,10-phenanthroline and dipicolinic acid. This hypothesis is further supported by the finding that the presence of substrate protects the enzymatic activity from dipicolinic acid inhibition. Furthermore the total cysteine residues per subunit were investigated by sulphydryl groups titrating agents.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins chemistry
Chelating Agents pharmacology
Cysteine analysis
Cytidine Deaminase antagonists & inhibitors
Cytidine Deaminase chemistry
Female
Humans
Molecular Sequence Data
Phenanthrolines pharmacology
Picolinic Acids pharmacology
Pregnancy
Sequence Alignment
Sequence Homology, Amino Acid
Sulfhydryl Compounds analysis
Cytidine Deaminase isolation & purification
Placenta enzymology
Zinc analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1039-9712
- Volume :
- 42
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemistry and molecular biology international
- Publication Type :
- Academic Journal
- Accession number :
- 9247704
- Full Text :
- https://doi.org/10.1080/15216549700202871