The two alkaline phosphatases for glycerophosphate in the rat's kidney

Gryder, Rosa M.; Friedenwald, Jonas S.; Carlson, Carolyn

doi:10.1016/0003-9861(55)90040-0

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1958

1979

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Cited by 24 publications

(2 citation statements)

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“…However, we can not exclude the possibility of the existence of more than one alkaline phosphatase. Results in support of this hypothesis have been published by Gomori (1952), Gryder, Friedenwald &Carlson (1955) andArai (1956). This question is now being studied.…”

supporting

confidence: 60%

Purification of kidney alkaline phosphatase

Alvarez

Lora‐Tamayo

1958

Biochemical Journal

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supporting

confidence: 60%

Purification of kidney alkaline phosphatase

Alvarez

Lora‐Tamayo

1958

Biochemical Journal

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“…Mg2+ sensitivity, EDTA, KCN and sodium deoxycholate inhibition have been examined in an attempt to elucidate this problem [11]. Variations in the solubility of the enzyme, bound more or less firmly to membrane or other structures, may play an important role.…”

Section: Discussionmentioning

confidence: 99%

The Ultrastructural Localization of Alkaline Phosphatase Isoenzymes in Some Normal and Malignant Cells

Lustig¹,

Ja²

1971

Enzyme

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(1) Alkaline phosphatases were present in all subcellular fractions obtained by ultracentrifugation of all the tissues examined. (2) The highest specific activities (mU/mg protein) were found in the microsomal fractions, the lowest in the supernatant, with the exception of the mammary tumour examined. (3) A different thermostability of the enzymes in the various fractions pointed to the presence of isoenzymes; a biphasic curve gave evidence of the simultaneous presence of at least two isoenzymes in some particulate structures. (4) There was no specific thermolabile pattern of alkaline phosphatases in the malignant tissues examined, assuming the method used is valid for establishing such differences.

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