Assays for glyoxylate aminotransferase activities

Rowsell, E. V.; Carnie, John; Snell, Keith; Taktak, B.

doi:10.1016/0020-711x(72)90036-5

Cited by 58 publications

(26 citation statements)

References 14 publications

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“…Assays: A C T (EC 2.6.1.44) was assayed by published methods (Rowsell et al, 1972;Nakatani et al, 1985) as was catalase (EC 1.11.1.6) (Baudhuin et al, 1964). Protein was determined by the method of Lowry et al (1951).…”

Section: Methodsmentioning

confidence: 99%

Primary hyperoxaluria type I: Ultrastructural observations in liver biopsies

Iancu

Danpure

1987

J of Inher Metab Disea

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The liver ultrastructure of four patients with the peroxisomal disease primary hyperoxaluria type I has been investigated. In all cases, peroxisomes of normal appearance were present in the parenchymal cells, except that they were somewhat reduced in number and size. In all patients, conspicuous lipofuscin was present, presumably resulting from the various metabolic disturbances to which the livers were subjected during the course of their disease. Considerable hepatocyte iron overloading was found in the three patients who had been hemodialyzed and/or had blood transfusions. Whether the relatively mild peroxisomal abnormalities (as compared to other peroxisomal diseases, such as Zellweger's syndrome) found in these hyperoxaluric patients are related directly to the peroxisomal deficiency of alanine:glyoxylate aminotransferase, or whether they are a secondary phenomenon, resulting from the consequent metabolic disturbance, remains to be elucidated.

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Section: Methodsmentioning

confidence: 99%

Primary hyperoxaluria type I: Ultrastructural observations in liver biopsies

Iancu

Danpure

1987

J of Inher Metab Disea

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“…Any non-suspended fibrous material was removed by low-speed centrifugation. Table 1 AGT activity and GGT activity were assayed by a modification of the method of Rowsell et al [6]. Protein was measured by the method of Lowry et al [7].…”

Section: Liversmentioning

confidence: 99%

Immunological heterogeneity of hepatic alanine:glyoxylate aminotransferase in primary hyperoxaluria type 1

Wise¹,

Danpure²,

Jennings³

1987

FEBS Letters

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Immunoblotting of human liver sonicates, after SDS-polyacrylamide gel electrophoresis, demonstrated the presence of a 40 kDa protein, corresponding to the subunit of alanineglyoxylate aminotransferase, in six controls and three patients with primary hyperoxaluria type 1 (peroxisomal alanineglyoxylate aminotransferase deficiency). This immunoreactive 40 kDa protein was absent in a further nine patients. Subcellular fractionation of patients' livers showed that the 40 kDa protein, when present, was located mainly in the peroxisomes. In a heteroxygote liver, the 40 kDa protein was also mainly peroxisomal and paralleled the distribution of alanine:glyoxylate aminotransferase activity.

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“…T. litoralis was grown as previously described (21). AGT activity was assayed by the method of Rowsell et al (24). Pyruvate formed by the AGT reaction was assayed by spectrophotometric NADH determination using lactate dehydrogenase (EC 1.1.1.27).…”

mentioning

confidence: 99%