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Human carbamoylphosphate synthetase I.
- Source :
-
Enzyme [Enzyme] 1981; Vol. 26 (5), pp. 233-9. - Publication Year :
- 1981
-
Abstract
- Carbamoylphosphate synthetase (ammonia) isolated from human liver has been characterized. It is composed of monomers (constituted by a single polypeptide of 160,000 +/- 5,000 Mr) that can associate into dimers, although in the native state the monomer predominates. Physical and kinetic properties and amino acid composition are very similar to those found for the rat liver enzyme. There is extensive immunological cross-reactivity between the enzymes from both species. These results are discussed in the light of a possible regulatory role of carbamoylphosphate synthetase. The implications of these findings on a number of pathological states are also discussed.
- Subjects :
- Amino Acid Metabolism, Inborn Errors enzymology
Amino Acids
Animals
Carbamoyl-Phosphate Synthase (Ammonia) immunology
Carbamoyl-Phosphate Synthase (Ammonia) isolation & purification
Chemical Phenomena
Chemistry
Humans
Infant, Newborn
Kinetics
Macromolecular Substances
Mitochondria, Liver enzymology
Protein Conformation
Species Specificity
Carbamoyl-Phosphate Synthase (Ammonia) metabolism
Ligases metabolism
Liver enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0013-9432
- Volume :
- 26
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Enzyme
- Publication Type :
- Academic Journal
- Accession number :
- 7028477
- Full Text :
- https://doi.org/10.1159/000459184