Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method

R. J. Wanders; J. Ruiter; C. W. van Roermund; R. B. Schutgens; R. Ofman; S. Jurriaans; J. M. Tager

doi:https://doi.org/10.1016/0009-8981(90)90084-6

Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method

R. J. Wanders, J. Ruiter, C. W. van Roermund, R. B. Schutgens, R. Ofman, S. Jurriaans, J. M. Tager

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Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

We have studied the characteristics of human liver alanine-glyoxylate aminotransferase, which is deficient in hyperoxaluria type I, an inherited disorder of glyoxylate metabolism. The enzyme was optimally active at pH 8.0 showing apparent Km values for L-alanine and glyoxylate of 8.3 and 1.3 mmol/l, respectively. Activity was found to proceed linearly for up to 4 h. Measurements under these optimal conditions enabled the biochemical diagnosis of hyperoxaluria type I to be made via enzyme activity measurements in percutaneous needle biopsy specimens of liver tissue

Original language	English
Pages (from-to)	139-144
Journal	Clinica chimica acta; international journal of clinical chemistry
Volume	189
Issue number	2
DOIs	https://doi.org/10.1016/0009-8981(90)90084-6
Publication status	Published - 1990

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https://doi.org/10.1016/0009-8981(90)90084-6

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Wanders, R. J., Ruiter, J., van Roermund, C. W., Schutgens, R. B., Ofman, R., Jurriaans, S., & Tager, J. M. (1990). Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method. Clinica chimica acta; international journal of clinical chemistry, 189(2), 139-144. https://doi.org/10.1016/0009-8981(90)90084-6

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title = "Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method",

abstract = "We have studied the characteristics of human liver alanine-glyoxylate aminotransferase, which is deficient in hyperoxaluria type I, an inherited disorder of glyoxylate metabolism. The enzyme was optimally active at pH 8.0 showing apparent Km values for L-alanine and glyoxylate of 8.3 and 1.3 mmol/l, respectively. Activity was found to proceed linearly for up to 4 h. Measurements under these optimal conditions enabled the biochemical diagnosis of hyperoxaluria type I to be made via enzyme activity measurements in percutaneous needle biopsy specimens of liver tissue",

author = "Wanders, {R. J.} and J. Ruiter and {van Roermund}, {C. W.} and Schutgens, {R. B.} and R. Ofman and S. Jurriaans and Tager, {J. M.}",

year = "1990",

doi = "https://doi.org/10.1016/0009-8981(90)90084-6",

language = "English",

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Wanders, RJ, Ruiter, J, van Roermund, CW, Schutgens, RB, Ofman, R , Jurriaans, S & Tager, JM 1990, 'Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method', Clinica chimica acta; international journal of clinical chemistry, vol. 189, no. 2, pp. 139-144. https://doi.org/10.1016/0009-8981(90)90084-6

Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method. / Wanders, R. J.; Ruiter, J.; van Roermund, C. W. et al.
In: Clinica chimica acta; international journal of clinical chemistry, Vol. 189, No. 2, 1990, p. 139-144.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method

AU - Wanders, R. J.

AU - Ruiter, J.

AU - van Roermund, C. W.

AU - Schutgens, R. B.

AU - Ofman, R.

AU - Jurriaans, S.

AU - Tager, J. M.

PY - 1990

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N2 - We have studied the characteristics of human liver alanine-glyoxylate aminotransferase, which is deficient in hyperoxaluria type I, an inherited disorder of glyoxylate metabolism. The enzyme was optimally active at pH 8.0 showing apparent Km values for L-alanine and glyoxylate of 8.3 and 1.3 mmol/l, respectively. Activity was found to proceed linearly for up to 4 h. Measurements under these optimal conditions enabled the biochemical diagnosis of hyperoxaluria type I to be made via enzyme activity measurements in percutaneous needle biopsy specimens of liver tissue

AB - We have studied the characteristics of human liver alanine-glyoxylate aminotransferase, which is deficient in hyperoxaluria type I, an inherited disorder of glyoxylate metabolism. The enzyme was optimally active at pH 8.0 showing apparent Km values for L-alanine and glyoxylate of 8.3 and 1.3 mmol/l, respectively. Activity was found to proceed linearly for up to 4 h. Measurements under these optimal conditions enabled the biochemical diagnosis of hyperoxaluria type I to be made via enzyme activity measurements in percutaneous needle biopsy specimens of liver tissue

U2 - https://doi.org/10.1016/0009-8981(90)90084-6

DO - https://doi.org/10.1016/0009-8981(90)90084-6

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JO - Clinica chimica acta; international journal of clinical chemistry

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Wanders RJ, Ruiter J, van Roermund CW, Schutgens RB, Ofman R , Jurriaans S et al. Human liver L-alanine-glyoxylate aminotransferase: characteristics and activity in controls and hyperoxaluria type I patients using a simple spectrophotometric method. Clinica chimica acta; international journal of clinical chemistry. 1990;189(2):139-144. doi: https://doi.org/10.1016/0009-8981(90)90084-6