Ectoenzyme release from rat liver and kidney by phosphatidylinositol-specific phospholipase C.

Abstract:

:Ectoenzyme release from rat liver and kidney by phosphatidylinositol (PI)-specific phospholipase C of Bacillus thuringiensis was studied. Alkaline phosphatase and 5'-nucleotidase were released from rat kidney slices to extents of up to 60% and 30%, respectively. Release of alkaline phosphatase was observed at lower amounts of PI-specific phospholipase C than that of 5'-nucleotidase. Both enzymes were more easily released from microsomal fractions or free cells. From kidney cells, alkaline phosphatase was released without cell lysis, and more than 80% release of alkaline phosphatase was observed at 3.8% hydrolysis of PI. Isoelectric focusing profiles of alkaline phosphatase released by PI-specific phospholipase C were significantly different from the control in the cases of both rat liver and kidney. Lubrol-solubilized alkaline phosphatase was eluted at the void volume of a Toyopearl HW-55 column, while the enzyme obtained by further treatment with PI-specific phospholipase C was eluted in the lower-molecular-weight region corresponding to 100,000-110,000 daltons. Furthermore, Lubrol-solubilized phosphatase became more thermostable on treatment with PI-specific phospholipase C.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Taguchi R,Asahi Y,Ikezawa H

doi

10.1093/oxfordjournals.jbchem.a135133

subject

Has Abstract

pub_date

1985-03-01 00:00:00

pages

911-21

issue

3

eissn

0021-924X

issn

1756-2651

journal_volume

97

pub_type

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