INTERACTION OF RABBIT MUSCLE ALDOLASE WITH PHOSPHOLIPID LIPOSOMES

被引：17

作者：

GUTOWICZ, J

MODRZYCKA, T

机构：

[1] Department of Biophysics, Institute of Biochemistry and Biophysics, Medical School, 50-368 Wrockław

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 554卷 / 02期

关键词：

(Rabbit muscle); Aldolase; Conformational change; Enzyme-lipid interaction; Fluorescence quenching; Liposome; Membrane-enzyme interaction;

D O I：

10.1016/0005-2736(79)90376-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction between rabbit muscle fructose diphosphate aldolase and phospholipid model membranes (liposomes) was studied by measurement of the tryptophan fluorescence of the enzyme. Interaction with liposomes decreases intrinsic fluorescence intensity of the enzyme and shifts the emission wavelength maximum to higher values. The effects appear to be strongly dependent on the nature of the phospholipid polar group and on ionic strength. Also, a reversible modification of specific activity of aldolase upon interaction with liposomes was found. It is postulated that aldolase binds to liposomes mainly by electrostatic interactions and that the binding causes a change in the conformation of the enzyme. © 1979.

引用

页码：358 / 363

页数：6

共 21 条

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[2]

BARTLETT GR, 1959, J BIOL CHEM, V234, P466

[3] SINGLE BILAYER VESICLES PREPARED WITHOUT SONICATION PHYSICOCHEMICAL PROPERTIES [J].