Kinetic and immunological differences between the retinal specific C4- and B4-lactate dehydrogenase of the cichlid fish Oreochromis mossambicus

Autor:	Yvette W. Kunz, Patrick Joyce, Jón M. Einarsson
Rok vydání:	1995
Předmět:	Gel electrophoresis Antiserum Oreochromis mossambicus Chromatography Physiology Dehydrogenase Biology biology.organism_classification Biochemistry Sepharose chemistry.chemical_compound chemistry DEAE-Sepharose Lactate dehydrogenase Protein purification Molecular Biology
Zdroj:	Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 112:589-598
ISSN:	1096-4959
DOI:	10.1016/0305-0491(95)00114-x
Popis:	The eye-specific C4-lactate dehydrogenase (LDH) and the widely distributed B4-LDH isozymes from the fish Oreochromis mossambicus were purified to homogeneity using DEAE Sepharose ion-exchange chromatography and oxamate-linked sepharose affinity-chromatography. Kinetic analysis was performed on pure B4- and C4-LDH. The Michaelis-Menten constant (Km) for B4-LDH and pyruvate was 32.3μM, for B4-LDH and lactate 717 μM for C4-LDH and pyruvate 14.1 μM and for C4-LDH and lactate 1898 μM. The pure C4-isozyme was subjected to SDS-polyacrylamide gel electrophoresis and the Coomassie Brilliant Blue-stained band injected into a rat to produce antiserum. The antiserum proved to be C4-LDH monospecific, which will allow using it to localize the isozyme in the retina at a light and electron microscopical level.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::946a802aa513211f97c1c4048ebf52b3 https://doi.org/10.1016/0305-0491(95)00114-x Zobrazit plný text záznamu Full Text from ScienceDirect