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Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization.
Nucleic Acids Research
|July 25, 1984
Summary
Researchers sequenced the human purine nucleoside phosphorylase (PNP) cDNA, revealing its 32 kDa protein structure. They also isolated and characterized the genomic organization of the wild-type human PNP gene using the cDNA clone.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Human purine nucleoside phosphorylase (PNP) is crucial for purine metabolism.
- Previous studies reported the isolation of a cDNA clone for human PNP.
Purpose of the Study:
- To determine the nucleotide sequence of the human PNP cDNA clone.
- To derive and compare the amino acid sequence with known composition.
- To isolate and characterize the genomic organization of the wild-type human PNP gene.
Main Methods:
- Nucleotide sequencing of the cDNA clone.
- Amino acid sequence derivation and comparison.
- Screening of a bacteriophage lambda library using a cDNA probe.
- Isolation and characterization of human PNP genomic clones.
Main Results:
- The nucleotide sequence of the human PNP cDNA was determined.
- The derived amino acid sequence corresponds to a 32 kilodalton protein.
- Genomic clones of the wild-type human PNP gene were isolated.
- The structural organization of the human PNP gene was elucidated.
Conclusions:
- The complete coding sequence and derived protein structure of human PNP are established.
- The genomic structure of the wild-type human PNP gene has been determined, providing insights into its organization.