Value of differential thermostability, urea inhibition, and gel filtration of alkaline phosphatase in the identification of disease states.

Fennelly, J. J.; FitzGerald, M. X.; McGeeney, K. F.

doi:10.1136/gut.10.1.45

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1970

1986

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Cited by 30 publications

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Alkaline phosphatase in meningiomas

Timperley¹,

Warnes²

1970

Cancer

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Alkaline phosphatase was extracted from 5 meningiomas, and several of its biochemical properties were compared with alkaline phosphatase from normal serum and extracts of small intestine. The meningioma phosphatases behaved in a reasonably homogeneous manner. They were virtually uninhibited by 0.05 M L‐phenylalanine and were remarkably heat sensitive. One molar urea produced a similar degree of inactivation to that obtained with alkaline phosphatase of normal serum. Electrophoretically the alkaline phosphatase of all meningiomas produced a single band moving at the same rate as the main band seen in normal serum.

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