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. 1977 Jul;60(1):122–126. doi: 10.1104/pp.60.1.122

Properties and Subcellular Distribution of Two Partially Purified Ornithine Transcarbamoylases in Cell Suspensions of Sugarcane 1

Edward Glenn a, Andrew Maretzki b
PMCID: PMC542560  PMID: 16660023

Abstract

The spatially separated forms of ornithine transcarbamoylase (EC 2.1.3.3) of different molecular weights coexist in sugarcane (Saccharum sp.). The smaller form of the enzyme (mol wt 79,000) appears to be cytoplasmic, while a larger form (mol wt 224,000) sedimented with mitochondria. The Km of the cytoplasmic enzyme for ornithine was 3.11 mm, while the enzyme in the mitochondrial fraction had a Km of 0.50 mm for this substrate; both enzymes had similar affinity for carbamoyl phosphate (0.12 mm). Characteristics of the smaller ornithine transcarbamoylase are in keeping with a predominantly catabolic function, those of the enzyme which sediments with mitochondria, with an anabolic function. Only the mitochondrial enzyme was regulated in vivo by exogenous arginine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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