J. Biol. Chem., Vol. 259, Issue 23, 14498-14504, Dec, 1984
Developmental profiles and properties of hepatic peroxisomal apo- and mitochondrial holoalanine:glyoxylate aminotransferase during chick embryogenesis
T Noguchi and S Fujiwara
Alanine:glyoxylate aminotransferase was present as the apoenzyme in the
peroxisomes and as the holoenzyme in the mitochondria in chick embryos. The
peroxisomal enzyme predominated in the early stage and gradually decreased
during embryonic development and disappeared after hatching. In contrast,
the mitochondrial enzyme gradually increased and predominated in the later
stage of chick embryos. Peroxisomal alanine:glyoxylate aminotransferase in
chick embryos was a single peptide with a molecular weight of about 40,000.
The enzyme differed from the mitochondrial enzyme in the embryos, and
mammalian alanine:glyoxylate aminotransferases 1 (with a molecular weight
of about 80,000 with two identical subunits) and 2 (with a molecular weight
of about 200,000 with four identical subunits) in molecular weights and
immunological properties. Mitochondrial alanine:glyoxylate aminotransferase
in chick embryos had an identical molecular weight and immunologically
cross-reacted with mammalian mitochondrial alanine:glyoxylate
aminotransferase 2. Pyridoxal 5'-phosphate dissociated easily from the
peroxisomal enzyme saturated with pyridoxal 5'-phosphate. Hepatic
aspartate:2-oxoglutarate aminotransferase and alanine:2-oxoglutarate
aminotransferase in chick embryos, and hepatic alanine:glyoxylate
aminotransferases in different animal species were all present as the
holoenzyme.
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