Developmental changes of aldehyde dehydrogenase isozymes in human livers: mitochondrial ALDH2 isozyme is expressed in fetal livers. 1990

A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
Department of Biochemical Genetics, Beckman Research Institute, City of Hope, Duarte, California 91010.

Previous reports suggested that the major cytosolic aldehyde dehydrogenase (ALDH1) was present in fetal and infant livers, but the major mitochondrial isozyme (ALDH2) was absent or severely diminished. Re-examination by means of starch gel electrophoresis followed by enzyme activity staining, and by means of dot blot immuno-hybridization of liver samples with known genotypes of the ALDH2 locus, indicated that both ALDH1 and ALDH2 genes are expressed in fetal and infant livers. In addition, ALDH4 isozyme was also observed. The results imply that a fetus with the 'usual' homozygous ALDH1(2)/ALDH1(2) genotype, but not one with the atypical ALDH1(2)/ALDH2(2) or ALDH2(2)/ALDH2(2), is capable of detoxifying acetaldehyde transferred from the mother.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D004592 Electrophoresis, Starch Gel Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium. Starch Gel Electrophoresis
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000444 Aldehyde Dehydrogenase An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70. D-Glucuronolactone Dehydrogenase,Aldehyde Dehydrogenase (NAD(+)),Aldehyde Dehydrogenase E1,Aldehyde Dehydrogenase E2,Aldehyde-NAD Oxidoreductase,Aldehyde NAD Oxidoreductase,D Glucuronolactone Dehydrogenase,Dehydrogenase, Aldehyde,Dehydrogenase, D-Glucuronolactone
D015151 Immunoblotting Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies. Dot Immunoblotting,Electroimmunoblotting,Immunoelectroblotting,Reverse Immunoblotting,Immunoblotting, Dot,Immunoblotting, Reverse,Dot Immunoblottings,Electroimmunoblottings,Immunoblottings,Immunoblottings, Dot,Immunoblottings, Reverse,Immunoelectroblottings,Reverse Immunoblottings

Related Publications

A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
January 1993, Human heredity,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
August 1995, Biochemical and biophysical research communications,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
July 1988, Laboratory investigation; a journal of technical methods and pathology,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
May 1983, The Journal of biological chemistry,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
January 1990, Progress in clinical and biological research,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
January 1983, Isozymes,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
June 2010, Frontiers in bioscience (Elite edition),
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
October 1981, Nihon juigaku zasshi. The Japanese journal of veterinary science,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
November 1983, American journal of human genetics,
A Yoshida, and A Shibuya, and V Davé, and M Nakayama, and A Hayashi
October 2016, The FEBS journal,
Copied contents to your clipboard!