Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement

A F Howie; J D Hayes; G J Beckett

doi:10.1016/0009-8981(88)90308-7

Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement

A F Howie, J D Hayes, G J Beckett

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

21 Citations (Scopus)

Abstract

Human acidic glutathione S-transferases (GST) have been purified from placenta, lung and erythrocytes. The purification protocol resulted in a high yield of pure protein for each tissue, when compared to previous procedures. An apparent subunit Mr of 24,800 was calculated for each of the acidic GST and each enzymes had a pI of 4.75. No immunochemical differences were detected between the acidic GST isolated from the three tissues. A specific and sensitive radioimmunoassay suitable for the measurement of human acidic GST in plasma or tissues is described.

Original language	English
Pages (from-to)	65-75
Number of pages	11
Journal	Clinica Chimica Acta
Volume	177
Issue number	1
DOIs	https://doi.org/10.1016/0009-8981(88)90308-7
Publication status	Published - 30 Sept 1988

Keywords

Erythrocytes/enzymology
Glutathione Transferase/blood
Humans
Lung/enzymology
Placenta/enzymology
Radioimmunoassay/methods
Sensitivity and Specificity

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abstract = "Human acidic glutathione S-transferases (GST) have been purified from placenta, lung and erythrocytes. The purification protocol resulted in a high yield of pure protein for each tissue, when compared to previous procedures. An apparent subunit Mr of 24,800 was calculated for each of the acidic GST and each enzymes had a pI of 4.75. No immunochemical differences were detected between the acidic GST isolated from the three tissues. A specific and sensitive radioimmunoassay suitable for the measurement of human acidic GST in plasma or tissues is described.",

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T1 - Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement

AU - Howie, A F

AU - Hayes, J D

AU - Beckett, G J

PY - 1988/9/30

Y1 - 1988/9/30

N2 - Human acidic glutathione S-transferases (GST) have been purified from placenta, lung and erythrocytes. The purification protocol resulted in a high yield of pure protein for each tissue, when compared to previous procedures. An apparent subunit Mr of 24,800 was calculated for each of the acidic GST and each enzymes had a pI of 4.75. No immunochemical differences were detected between the acidic GST isolated from the three tissues. A specific and sensitive radioimmunoassay suitable for the measurement of human acidic GST in plasma or tissues is described.

AB - Human acidic glutathione S-transferases (GST) have been purified from placenta, lung and erythrocytes. The purification protocol resulted in a high yield of pure protein for each tissue, when compared to previous procedures. An apparent subunit Mr of 24,800 was calculated for each of the acidic GST and each enzymes had a pI of 4.75. No immunochemical differences were detected between the acidic GST isolated from the three tissues. A specific and sensitive radioimmunoassay suitable for the measurement of human acidic GST in plasma or tissues is described.

KW - Erythrocytes/enzymology

KW - Glutathione Transferase/blood

KW - Humans

KW - Lung/enzymology

KW - Placenta/enzymology

KW - Radioimmunoassay/methods

KW - Sensitivity and Specificity

U2 - 10.1016/0009-8981(88)90308-7

DO - 10.1016/0009-8981(88)90308-7

M3 - Article

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SN - 0009-8981

VL - 177

SP - 65

EP - 75

JO - Clinica Chimica Acta

JF - Clinica Chimica Acta

IS - 1

ER -

Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement

Abstract

Keywords

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