Alcohol dehydrogenase observed in separation of creatine kinase isoenzymes by electrophoresis

Autor:	Kyoko Akano, Tatsuo Tozawa
Rok vydání:	1998
Předmět:	Ethanol biology Mitochondrion medicine.disease Molecular biology Fluorescence chemistry.chemical_compound Electrophoresis chemistry Biochemistry Lactate dehydrogenase biology.protein medicine Creatine kinase Aplastic anemia Alcohol dehydrogenase
Zdroj:	SEIBUTSU BUTSURI KAGAKU. 42:57-60
ISSN:	1349-9785 0031-9082
Popis:	We found the fluorescent band revealed to cathodal position than mitochondria creatine kinase (CK) using the method of fluorescent staining (TAITAN N-CK, Helena) on CK electrophoresis, when we examined the serum of a patient with aplastic anemia who have been in serious liver damage (because of appearing graft versus host disease after bone marrow transplantation). However, it is widely noted that the alcohol dehydrogenase (ADH) band is believed to more cathodal position than lactate dehydrogenase (LDH) 5 on LDH electrophoresis. In this study, the fluorescent band revealed to cathodal position than mitochondria CK was also shown without substrate and addition of ethanol enhanced fluorescent strength. From these observations, these results suggest that this abnormal CK band will be ADH.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f28d77a15d7f711a42db78529c18149d https://doi.org/10.2198/sbk.42.57 Zobrazit plný text záznamu