Jan 1, 1975

Properties of plasma membranes from granulation tissue with reference to extracellular matrix

Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry
P LehtinenE Kulonen


Treatment with neuraminidase decreased the activity of Na+,K+-activated Mg2+-adenosine triphosphatase in plasma membranes isolated from experimental granulation tissue but not that of 5'-nucleotidase or leucine-beta-naphthylamidase. A temporary lowering of the pH of the plasma membrane suspension to 2-3 inactivated all three enzymes, which remained inactive after the pH had been readjusted to 7.4. Addition of dextran preparations to the membrane suspension decreased the activity of adenosine triphosphatase. Ethanol (0.4%) had a similar effect. These marker enzymes of plasma membranes were not affected by additions of hyaluronate, chondroitin sulfate, protein polysaccharide or soluble collagen. Serotonin stimulated the adenosine triphosphatase activity slightly. About 10-20% of the protein in the plasma membrane preparation was extracted with EDTA. This "fuzzy coat" fraction yielded a distinct gel-electrophoretic protein pattern. Hyaluronidase was not helpful in cleaving this surface layer from the plasma membranes.

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Mentioned in this Paper

Methoxyleucine Aminopeptidase
Granulation Tissue
Edetic Acid, Sodium Salt
DNA-dependent ATPase
Hydrogen-Ion Concentration
Enzyme Activation
Plasma Membrane

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