Further Evidence for a Separate Enzymic Entity for the Synthesis of Homocitrulline, Distinct from the Regular Ornithine Transcarbamylase
| Autor: | Hommes Fa, Metoki K, Rufo S, Eller Ag, Carter Al |
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| Rok vydání: | 1984 |
| Předmět: |
Male
Ornithine Lysine Ornithine transcarbamylase Mitochondria Liver Mitochondrion complex mixtures Biochemistry Mice chemistry.chemical_compound Animals Inner mitochondrial membrane Ornithine Carbamoyltransferase Homocitrulline Glutamate dehydrogenase Hydrogen-Ion Concentration Mice Mutant Strains Rats Kinetics Digitonin chemistry Citrulline bacteria Female |
| Zdroj: | Enzyme. 32:26-36 |
| ISSN: | 2504-2564 0013-9432 |
| DOI: | 10.1159/000469447 |
| Popis: | Differential digitonin extraction of rat liver mitochondria and of mitochondria of livers of affected and unaffected male sparse fur mice released a lysine transcarbamylase activity from the mitochondria at a digitonin to protein ratio in between that for myokinase and glutamate dehydrogenase, but at a slightly lower ratio than the ornithine transcarbamylase activity. Homocitrulline formation by isolated rat liver mitochondria is independent of the uptake of lysine by mitochondria as evidenced by the insensitivity of homocitrulline formation to changes in the matrix pH, in contrast to citrulline formation from ornithine. High-performance liquid chromatography separates the lysine transcarbamylase activity from the ornithine transcarbamylase activity. It is concluded that the lysine transcarbamylase activity is localized outside the inner mitochondrial membrane. |
| Databáze: | OpenAIRE |
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