Comparative immunochemical studies of carbonic anhydrase III in horses and other mammalian species.
Abstract: 1. Carbonic anhydrase III (CA-III) from different mammalian species (horse, cow, dog, cat, rat and rabbit) has been analyzed by the immunodiffusion technique with anti-equine CA-III serum. 2. Immunodiffusion demonstrated the absence of cross-reactivity between isozyme CA-I, CA-II, and CA-III. 3. Cross-reactions were observed between the CA-III from all the species examined except the rabbit. 4. Molecular weights and isoelectric points of CA-III from different species were determined by Western blotting.
Publication Date: 1988-01-01 PubMed ID: 3143514DOI: 10.1016/0305-0491(88)90118-6Google Scholar: Lookup
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- Comparative Study
- Journal Article
Summary
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The study explores the variation of the enzyme Carbonic Anhydrase III (CA-III) in various mammalian species like horses, cows, dogs, cats, rats, and rabbits, using comparative immunochemical methods. It reveals differences and similarities in the enzyme’s properties across these species, also showing no cross-reactivity among different Carbonic Anhydrase isozymes.
Objective of the Study
- The primary purpose of this research was to study and understand the nature of the enzyme Carbonic Anhydrase III (CA-III) across different mammalian species.
Methodology
- The researchers adopted the immunodiffusion technique to analyze CA-III from various animal species. The study specifically used anti-equine CA-III serum for the process.
- The researchers conducted their experiments on several species, including horses, cows, dogs, cats, rats, and rabbits to have a wide comparative perspective.
- Immunodiffusion was used not only to compare across species but also to investigate the cross-reactivity between different isozymes of Carbonic Anhydrase (CA-I, CA-II and CA-III).
- After the immunodiffusion tests, molecular weights and isoelectric points of the CA-III enzyme of the different species were determined through Western blotting.
Findings
- Immunodiffusion tests showed a lack of cross-reactivity between the isozyme forms of Carbonic Anhydrase, namely CA-I, CA-II, and CA-III. This suggests that these isozymes may function independently of each other.
- The study found cross-reactions between the CA-III enzymes taken from all the species, barring the rabbit. This implies some sort of similarity or commonality among these species regarding this enzyme, which is distinctly absent in rabbits.
- Through Western blotting, the researchers were also able to determine the molecular weights and isoelectric points of the CA-III enzyme from the different species. The differences or similarities in these properties could give insight into the evolutionary or functional differences of CA-III between these species.
Cite This Article
APA
Nishita T, Matsushita H.
(1988).
Comparative immunochemical studies of carbonic anhydrase III in horses and other mammalian species.
Comp Biochem Physiol B, 91(1), 91-96.
https://doi.org/10.1016/0305-0491(88)90118-6 Publication
Researcher Affiliations
- Laboratory of Veterinary Physiology, School of Veterinary Medicine, Azabu University, Kanagawa, Japan.
MeSH Terms
- Animals
- Carbonic Anhydrases / immunology
- Cats
- Cattle
- Cross Reactions
- Dogs
- Female
- Horses / metabolism
- Immunochemistry
- Isoelectric Point
- Male
- Molecular Weight
- Rabbits
- Rats
- Species Specificity
Citations
This article has been cited 6 times.- Nishita T, Yatsu J, Murakami M, Kamoshida S, Orito K, Ichihara N, Arishima K, Ochiai H. Isolation and sequencing of swine carbonic anhydrase VI, an enzyme expressed in the swine kidney.. BMC Res Notes 2014 Feb 28;7:116.
- Nishita T, Yorifuji D, Orito K, Ichihara N, Arishima K. Muscle carbonic anhydrase III levels in normal and muscular dystrophia afflicted chickens.. Acta Vet Scand 2012 May 29;54(1):34.
- Nishita T, Tomita Y, Yorifuji D, Orito K, Ochiai H, Arishima K. Purification of chicken carbonic anhydrase isozyme-III (CA-III) and its measurement in White Leghorn chickens.. Acta Vet Scand 2011 Nov 26;53(1):63.
- Nishita T, Arishima K, Yamamoto M, Matsushita H. Evidence for the presence of carbonic anhydrase III in the myoid cells of the bovine thymus. Immunocytochemical and ultrastructural study.. Histochemistry 1989;92(1):87-8.
- Nishita T, Oshige H, Matsushita H, Kano Y, Asari M. The immunohistolocalization of carbonic anhydrase III in the submandibular gland of rats and hamsters.. Histochem J 1989 Jan;21(1):8-14.
- Nishita T, Matsushita H. Immunocytochemical localization of carbonic anhydrase isozyme III in equine thymus.. Histochemistry 1989;91(1):39-42.
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