Escherichia coli photoreactivating enzyme: purification and properties

Journal Article · Tue Jan 01 04:00:00 EST 1980 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00559a010· OSTI ID:5727002

Snapka, R M; Sutherland, B M

Researchers have purified large quantities of Escherichia coli photoreactivating enzyme to apparent homogeneity and have studied its physical and chemical properties. The enzyme has a molecular weight of 36,800 and a S/sub 20,w//sup 0/ of 3.72 S. Amino acid analysis revealed an apparent absence of tryptophan, a low content of aromatic residues, and the presence of no unusual amino acids. The N terminus is arginine. The purified enzyme contained up to 13% carbohydrate by weight. The carbohydrate was composed of mannose, galactose, glucose, and N-acetylglucosamine. The enzyme is also associated with RNA containing uracil, adenine, guanine, and cytosine with no unusual bases detected.

• OSTI ID: 5727002
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 19:18; ISSN BICHA
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
BACTERIA
BINDING ENERGY
BIOLOGICAL EFFECTS
BIOLOGICAL RADIATION EFFECTS
BIOLOGICAL RECOVERY
BIOLOGICAL REPAIR
CHEMICAL COMPOSITION
CHEMICAL PROPERTIES
DNA
ELECTROMAGNETIC RADIATION
ELECTROPHORESIS
ENERGY
ENZYMES
ESCHERICHIA COLI
MEASURING METHODS
MICROORGANISMS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PHOTOREACTIVATION
RADIATION EFFECTS
RADIATIONS
RECOVERY
REPAIR
RNA
STRUCTURAL CHEMICAL ANALYSIS
ULTRAVIOLET RADIATION