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Molecular cloning of a cDNA encoding human histidase
1Department of Pediatrics, Nagoya City University Medical School, Aichi, Japan.
Biochimica Et Biophysica Acta
|November 16, 1993
Summary
Researchers isolated human histidase (histidine ammonia-lyase) cDNA, revealing a 657 amino acid protein. This human enzyme shows high sequence conservation with rodent counterparts, suggesting conserved function.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Histidase (histidine ammonia-lyase) is a key enzyme in histidine metabolism.
- Understanding the human enzyme's structure and function is crucial for metabolic research.
Purpose of the Study:
- To isolate and characterize the cDNA encoding human histidase.
- To determine the predicted amino acid sequence and identify conserved features.
Main Methods:
- Isolation of overlapping cDNA clones from a human lambda gt10 library.
- Sequence analysis to predict protein characteristics.
Main Results:
- Successfully isolated cDNA clones for human histidase.
- Predicted a protein of 657 amino acids and 72,651 Da.
- Identified 93% amino acid sequence conservation with rat and mouse histidase, including four N-glycosylation sites.
Conclusions:
- The human histidase gene has been cloned and characterized.
- High sequence conservation suggests conserved functional roles across mammalian species.
- The presence of N-glycosylation sites indicates potential post-translational modifications.