TY - JOUR
T1 - An immunochemical study of δ-aminolevulinate synthase and δ-aminolevulinate dehydratase in liver and erythroid cells of rat
AU - Yamamoto, Masayuki
AU - Fujita, Hiroyoshi
AU - Watanabe, Norimichi
AU - Hayashi, Norio
AU - Kikuchi, Goro
N1 - Funding Information:
’ This work was supported in part by grants from the Ministry of Education, Science and Culture, Japan (Grant-in-Aid for Scientific Research) and from the Ministry of Health and Welfare, Japan (The Research Grant for the Intractable Diseases). z Present address: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Ill. 60201. ’ To whom correspondence should be addressed.
PY - 1986/2/15
Y1 - 1986/2/15
N2 - The relationship between erythroid δ-aminolevulinate (ALA) synthase and hepatic ALA synthase in rat was analyzed immunochemically, using antibodies directed against rat liver ALA synthase and against chicken liver ALA synthase. Rat erythroid ALA synthase showed no cross-reactivity with anti-liver ALA synthase antibodies, but hepatic ALA synthases from rat, mouse, and chicken share substantial cross-reactivity with one another. These results clearly distinguish the isozyme relationship between erythroid ALA synthase and hepatic ALA synthase in rat and suggest that there may be at least two different ALA synthase genes in rat. ALA dehydratase in rat liver, on the other hand, could not be immunochemically distinguished from ALA dehydratase in rat erythroid cells when antibody against rat erythroid ALA dehydratase was used. The finding that erythroid ALA synthase is an entity different from hepatic ALA synthase may provide a clue to understanding the different features in hepatic and erythropoietic porphyrias.
AB - The relationship between erythroid δ-aminolevulinate (ALA) synthase and hepatic ALA synthase in rat was analyzed immunochemically, using antibodies directed against rat liver ALA synthase and against chicken liver ALA synthase. Rat erythroid ALA synthase showed no cross-reactivity with anti-liver ALA synthase antibodies, but hepatic ALA synthases from rat, mouse, and chicken share substantial cross-reactivity with one another. These results clearly distinguish the isozyme relationship between erythroid ALA synthase and hepatic ALA synthase in rat and suggest that there may be at least two different ALA synthase genes in rat. ALA dehydratase in rat liver, on the other hand, could not be immunochemically distinguished from ALA dehydratase in rat erythroid cells when antibody against rat erythroid ALA dehydratase was used. The finding that erythroid ALA synthase is an entity different from hepatic ALA synthase may provide a clue to understanding the different features in hepatic and erythropoietic porphyrias.
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U2 - 10.1016/0003-9861(86)90191-8
DO - 10.1016/0003-9861(86)90191-8
M3 - Article
C2 - 3080960
AN - SCOPUS:0022529689
SN - 0003-9861
VL - 245
SP - 76
EP - 83
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -