Study of Carbamyl Phosphate-Ornithine Transcarbamylase

Burnett, George H.; Cohen, Philip P.

doi:10.1016/s0021-9258(18)70620-0

Cited by 81 publications

(5 citation statements)

References 10 publications

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“…The results of the present work are in general agreement with the findings of Burnett & Cohen (1957) and Reichard (1957), with oxand rat-liver preparations respectively (Table 2). Since our preparation was obtained by a different isolation procedure the similarity of enzyme properties suggests that the contaminating protein is not having.…”

Section: Discussionsupporting

confidence: 93%

“…The values found were forKa,, andforKb,, Product inhibition. Significant inhibition of the I X reaction by citrulline occurs only at very high con-10 / 20 30 centrations (Burnett & Cohen, 1957) and for this Time (min.) reason was not studied.…”

Section: Properties Of Ornithine Carbamoyltransferasementioning

confidence: 64%

“…appears to be about 40 % more active than that of Burnett & Cohen (1957), after the difference in the ionic strength of the assay system has been allowed for, and less pure than that of Reichard (1957).…”

Section: Discussionmentioning

confidence: 88%

“…has been partially purified from rat liver (Grisolia & Cohen, 1952;Reichard, 1957), from ox liver (Burnett & Cohen, 1957) and from Streptococcus lacts (Ravel, Grona, Humphreys & Shive, 1959). Some properties of the enzyme have been studied and certain differences between the preparations have been observed.…”

mentioning

confidence: 99%

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Studies on carbamoyl phosphate-l-ornithine Carbamoyltransferase from ox liver

Joseph¹,

Baldwin²,

Watts³

1963

Biochemical Journal

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Section: Discussionsupporting

confidence: 93%

Section: Properties Of Ornithine Carbamoyltransferasementioning

confidence: 64%

Section: Discussionmentioning

confidence: 88%

mentioning

confidence: 99%

See 2 more Smart Citations

Studies on carbamoyl phosphate-l-ornithine Carbamoyltransferase from ox liver

Joseph¹,

Baldwin²,

Watts³

1963

Biochemical Journal

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“…Ornithine transcarbamylase was partially purified from fresh calf liver according to the procedure of Burnett and Cohen (1957). The enzyme was purified up to the ammonium sulfate fractionation step described by these authors.…”

Section: Methodsmentioning

confidence: 99%

Isolation and identification of L-β-aspartyl-L-lysine and L-γ-glutamyl-L-ornithine from normal human urine

Lou¹

1975

Biochemistry

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L-beta-Aspartyl-L-lysine and L-gamma-glutamyl-L-ornithine were isolated from pooled normal human urine and each peptide was shown to be identical with the authentic peptides. The concentrations of these dipeptides in the urine of individual subjects were determined directly by using a new buffer sequence on a standard ion exchange chromatographic amino acid analyzer with a sensitivity of 10(-10) mol. In urine from normal subjects ranging in age from 12 to 64 years, mean values of 1.47 mumol/g of creatinine of L-gamma-glutamyl-L-ornithine and 8,24 mumol/g of creatinine of L-beta-aspartyl-L-lysine were found. The urine of children under 10 years of age contained, relative to creatinine excretion, more L-beta-aspartyl-L-lysine and L-gamma-glutamyl-L-ornithine than that of older children and adults. All urines contained substantially larger concentrations of L-beta-aspartyl-L-lysine than of L-gamma-glutamyl-L-ornithine. Both peptides were found in urine collected after 21 hr of fasting in lower concentrations than found in urine from nonfasting subjects. The urinary concentrations of both peptides did not appear to be influenced by race or sex.

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Genetically Controlled Differences in Enzyme Activity

Fincham

1960

Advances in Enzymology - And Related Areas of Molecular Biology

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Study of Carbamyl Phosphate-Ornithine Transcarbamylase

Cited by 81 publications

References 10 publications

Studies on carbamoyl phosphate-l-ornithine Carbamoyltransferase from ox liver

Studies on carbamoyl phosphate-l-ornithine Carbamoyltransferase from ox liver

Isolation and identification of L-β-aspartyl-L-lysine and L-γ-glutamyl-L-ornithine from normal human urine

Genetically Controlled Differences in Enzyme Activity

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