Literature DB >> 12813568

The influence of metmyoglobin and ferrylmyoglobin on the human erythrocyte membrane.

Małgorzata Sztiller1, Mieczysław Puchała.   

Abstract

Preliminary experiments revealed that ferrylmyoglobin decayed more slowly in the absence than in the presence of intact erythrocytes and erythrocyte membranes. This suggested the existence of interactions between FerrylMb and the erythrocyte membrane. Subsequent studies examined the influence of FerrylMb on the membrane of intact erythrocytes and on isolated erythrocyte membranes. The incubation of intact erythrocytes with FerrylMb did not influence their osmotic fragility or the fluidity of their membranes; the level of peroxidation of the membrane lipids increased only slightly (there was only a slight increase in the level of membrane lipid peroxidation). The activity of acetylcholinesterase significantly increased after 15 minutes of incubation, whereas longer incubation did not lead to any changes in the activity of this enzyme. The incubation of isolated erythrocyte membranes with FerrylMb resulted in an increase in their fluidity and a significant rise in the level of lipid peroxidation.

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Year:  2003        PMID: 12813568

Source DB:  PubMed          Journal:  Cell Mol Biol Lett        ISSN: 1425-8153            Impact factor:   5.787


  1 in total

1.  Effect of human serum albumin upon the permeabilizing activity of sticholysin II, a pore forming toxin from Stichodactyla heliantus.

Authors:  Gloria Celedón; Gustavo González; Felipe Gulppi; Fabiola Pazos; María E Lanio; Carlos Alvarez; Cristian Calderón; Rodrigo Montecinos; Eduardo Lissi
Journal:  Protein J       Date:  2013-12       Impact factor: 2.371

  1 in total

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