Erratum to: Identification of Human Erythrocyte Cytosolic Proteins Associated with Plasma Membrane During Thermal Stress

Erratum to: J Membrane Biol DOI 10.1007/s00232-013-9569-0

The original version of this article unfortunately contains an error. The presentation of Figs. 4, 5 and 6 are incorrect, and erroneously altered during proof correction. The corrected figures and their captions are given below.

Fig. 4

Analysis of erythrocyte lysate (cytosol) and membrane proteins obtained from erythrocyte cell suspension exposed to various temperatures by SDS-PAGE (12 % gel) and stained with CBB. Lane 1 unheated erythrocytes (whole cells, UnHEs); lane 2 unheated erythrocyte lysate (UnHEsCy); lanes 3–6 lysates (HEsCy) obtained from heat-stressed erythrocytes exposed to 44, 46, 48 and 50 °C for 15 min, respectively (60 μl protein in each lane); lane 7 unheated erythrocyte membrane (UnHEMs); lanes 8–11 erythrocyte membranes (HEMs) obtained from heat-stressed erythrocytes exposed to 44, 46, 48 and 50 °C for 15 min, respectively (60 μg protein in each lane). This is a representative pattern obtained for four different samples

Fig. 5

Analysis of Triton shells obtained from erythrocyte membranes exposed to various temperatures. a Separation of proteins of Triton shells obtained from unheated (UnHEMs) and heat-stressed (HEMs) erythrocyte membranes by SDS-PAGE (12 % gel) and stained with CBB followed by mass spectrometric identification (Table 2). Lane 1 unheated erythrocytes (whole cells, UnHEs, 60 μl); lane 2 unheated erythrocyte lysate (UnHEsCy, 60 μl); lane 3 unheated erythrocyte membrane (UnHEMs, 60 μg); lanes 4–8 Triton shells obtained from unheated (UnHEsTS) and heat-stressed (HEsTS) erythrocytes exposed to 44, 46, 48 and 50 °C for 15 min, respectively (50 μg protein in each lane); lane 9 membranes (HEMs) from heat-stressed erythrocytes exposed to 50 °C for 15 min (60 μg). b Densitometric spectra of UnHEsTS (red peaks) and HEsTS (green peaks). c Bar diagram shows changes in protein intensity (n = 4). The data are mean ± SE (n = 4). Upper symbol indicates the differences versus control (UnHEsTS). *p<0.05, **p<0.01, ***p<0.001; ns nonsignificant (Color figure online)

Fig. 6

Analysis of interactions of Triton shells and cytosolic proteins obtained from unheated erythrocytes (UnHEs) under heat stress. a Separation of proteins of Triton shells interacted with cytosolic proteins under heat stress by SDS-PAGE (12 % gel) and stained with CBB followed by mass spectrometric identification (Table 3). Lane 1 unheated erythrocytes (whole cells, 60 μl); lane 2 unheated erythrocyte lysate (60 μl); lane 3 unheated erythrocyte membrane (60 μg); lane 4 Triton shells obtained from unheated erythrocyte membrane (50 μg); lanes 5–9 Triton shells (derived from unheated erythrocyte membranes) were incubated with the unheated lysate at 0, 44, 46, 48 and 50 °C for 15 min, respectively (50 μg protein in each lane); Lane 10 Membranes from heat-stressed erythrocytes exposed to 50 °C for 15 min. (60 μg). b Densitometric spectra of UnHEsTS (red peaks) and UnHEsTS + Cy (green peaks). c Bar diagram shows changes in protein intensity (n = 4). The data are mean ± SE (n = 4). Upper symbol indicates the differences versus control (UnHEsTS). *p < 0.05, **p < 0.01, ***p < 0.001; ns nonsignificant (Color figure online)