Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
Abstract: The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isozyme, with 224 of the 259 residues being identical.
Publication Date: 1984-04-01 PubMed ID: 6428393DOI: 10.1007/BF00484234Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research paper discusses the investigation into the amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase, noting two different forms and its homology to the human carbonic anhydrase isozyme.
Research Objective and Methodology
- The objective of the study was to determine the amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II).
- This is sparked by the fact that carbonic anhydrase (CA) is a crucial enzyme in biology, playing important roles in various biochemical processes such as respiration and electrolyte balance.
- Equine erythrocyte CA represents a fascinating model for studying homologous enzymes and understanding their functional diversity and how slight sequence variations may impact function and activity.
- Using biochemical techniques, the researchers were able to isolate this enzyme and determine its sequence structure.
Key Findings
- The study found two different N-termini in the CA-II enzyme. These are referred to as the C1 and C2 forms. The C1 form has an N-acetyl-serine, while the C2 form has an N-acetyl-threonine.
- The N-terminal polymorphisms show how even in closely related species, slight modifications can present and these may potentially alter protein function.
- The sequence of the equine enzyme largely resembles the human CA-II isozyme. Out of the 259 residues, 224 were found to be identical. This level of homology reinforces the conserved nature of CA isozyme sequences throughout mammalian species.
- This high-level of similarity can be used to shed light on the human enzyme’s function and potentially the roles it plays in disease states.
Significance of Results
- The established sequence of equine erythrocyte CA and its comparison to the human homologue provides a deeper understanding of this critical enzyme, contributing to broader biochemical and physiological understanding.
- This could be useful for the development of therapeutic targets, as abnormal CA activity is associated with various diseases and conditions.
Cite This Article
APA
Jabusch JR, Deutsch HF.
(1984).
Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes.
Biochem Genet, 22(3-4), 357-367.
https://doi.org/10.1007/BF00484234 Publication
Researcher Affiliations
MeSH Terms
- Amino Acid Sequence
- Animals
- Carbonic Anhydrases / blood
- Carbonic Anhydrases / genetics
- Cattle
- Erythrocytes / enzymology
- Horses / blood
- Horses / genetics
- Humans
- Isoenzymes / genetics
- Mice
- Polymorphism, Genetic
- Rabbits
- Species Specificity
Grant Funding
- CA-1786 / NCI NIH HHS
References
This article includes 16 references
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