Isolation of a peroxidatically active product from the peptic digest of ox-liver catalase and some of its properties
- PMID: 5326719
- PMCID: PMC1264766
- DOI: 10.1042/bj0970827
Isolation of a peroxidatically active product from the peptic digest of ox-liver catalase and some of its properties
Abstract
1. A homogeneous peroxidatically active product has been isolated from a peptic digest of ox-liver catalase. 2. The nitrogen and the iron contents of the ;active product' are 15.3% and 0.21% respectively. 3. The S(0) (20,w) and molecular weight of the ;active product' are 2.6s and 27500 respectively. 4. The ;active product' contains 248 amino acid residues/mol. assuming a mol.wt. of 27500. 5. The properties of the ;active product' and catalase are compared and the relationship between their structures and enzyme activity is discussed.
Similar articles
-
Effect of some chemical modifications on the biological activity of catalase.Indian J Biochem. 1965 Jun;2(2):76-9. Indian J Biochem. 1965. PMID: 4221007 No abstract available.
-
The sulfatase of ox liver. X. Some observations on the intermolecular bonding in sulfatase A.Biochemistry. 1966 Apr;5(4):1379-88. doi: 10.1021/bi00868a035. Biochemistry. 1966. PMID: 5958212 No abstract available.
-
The isolation and properties of phenylalanine hydroxylase from rat liver.Biochem J. 1974 Jun;139(3):731-9. doi: 10.1042/bj1390731. Biochem J. 1974. PMID: 4854920 Free PMC article.
-
Superoxide and evolution.Horiz Biochem Biophys. 1974;1:1-37. Horiz Biochem Biophys. 1974. PMID: 4377564 Review. No abstract available.
-
[Electron structure of the hematin iron of catalase].Seikagaku. 1969 Mar;41(3):111-22. Seikagaku. 1969. PMID: 4892621 Review. Japanese. No abstract available.
Cited by
-
The effect of trypsin digestion on the activities of polynucleotide phosphorylase.Biochem J. 1967 Oct;105(1):25-33. doi: 10.1042/bj1050025. Biochem J. 1967. PMID: 6056626 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources