Characterization of cDNA clones encoding rabbit and human serum paraoxonase: The mature protein retains its signal sequence
- Univ. of Washington, Seattle (United States)
- W.Alton Jones Cell Science Center, Lake Placid, NY (United States)
Serum paraoxonase hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. High serum paraoxonase levels appear to protect against the neurotoxic effects of organophosphorus substrates of this enzyme. The amino acid sequence accounting for 42% of rabbit paraoxonase was determined. From these data, two oligonucleotide probes were synthesized and used to screen a rabbit liver cDNA library. Human paraoxonase clones were isolated from a liver cDNA library by using the rabbit cDNA as a hybridization probe. Inserts from three of the longest clones were sequenced, and one full-length clone contained an open reading frame encoding 355 amino acids, four less than the rabbit paraoxonase protein. Amino-terminal sequences derived from purified rabbit and human paraoxonase proteins suggested that the signal sequence is retained, with the exception of the initiator methionine residue. Characterization of the rabbit and human paraoxonase cDNA clones confirms that the signal sequences are not processed, except for the N-terminal methionine residue. The rabbit and human cDNA clones demonstrate striking nucleotide and deduced amino acid similarities (greater than 85%), suggesting an important metabolic role and constraints on the evolution of this protein.
- OSTI ID:
- 5488538
- Journal Information:
- Biochemistry; (United States), Vol. 30:42; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
DNA
AUTORADIOGRAPHY
ESTERASES
AMINO ACID SEQUENCE
INSECTICIDES
METABOLISM
RECOMBINANT DNA
DNA SEQUENCING
BIOLOGICAL EVOLUTION
MAN
RABBITS
ANIMALS
ENZYMES
HYDROLASES
MAMMALS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PESTICIDES
PRIMATES
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques