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Nucleotide sequence of a cDNA clone for human aldolase B
Biochemical and Biophysical Research Communications
|December 16, 1983
Summary
Researchers identified human aldolase B clones from a liver cDNA library. Sequence analysis revealed 92% homology between human and rat aldolase B C-terminal protein sequences.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Aldolase B is a key enzyme in glycolysis and gluconeogenesis.
- Understanding human aldolase B is crucial for metabolic research.
Purpose of the Study:
- To isolate and characterize human aldolase B cDNA clones.
- To determine the C-terminal amino acid sequence of human aldolase B.
- To compare the human sequence with its rat counterpart.
Main Methods:
- Screening a human liver cDNA library using a rat aldolase B cDNA probe.
- Hybridization-selection for clone identification.
- Nucleotide sequencing of the identified clone.
- Amino acid sequence analysis and homology comparison.
Main Results:
- Two specific clones for human aldolase B were successfully isolated.
- One clone was sequenced, allowing deduction of 127 C-terminal residues.
- Human aldolase B exhibited 92% amino acid homology with rat aldolase B.
Conclusions:
- The study provides valuable sequence data for human aldolase B.
- High homology suggests conserved function between human and rat aldolase B.
- This research aids in comparative genomics and understanding enzyme evolution.