Erythrocyte membrane protein analysis by sodium dodecyl sulphate-capillary gel electrophoresis in the diagnosis of hereditary spherocytosis

2011 ◽  
Vol 49 (3) ◽  
Author(s):  
France Debaugnies ◽  
Frédéric Cotton ◽  
Charles Boutique ◽  
Béatrice Gulbis
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Hereditary Spherocytosis ◽  
Sodium Dodecyl ◽  
Protein Analysis ◽  
Erythrocyte Membrane Protein ◽  
Capillary Gel Electrophoresis

scholarly journals Identification of the protein responsible for pyruvate transport into rat liver and heart mitochondria by specific labelling with [3H]N-phenylmaleimide

1981 ◽  
Vol 196 (2) ◽  
pp. 471-479 ◽  
Author(s):  
A P Thomas ◽  
A P Halestrap
Keyword(s):  
Membrane Protein ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mitochondrial Protein ◽  
Sodium Dodecyl ◽  
Liver Mitochondria ◽  
Heart Mitochondria ◽  
Approximate Amount ◽  
Specific Labelling

1. N-Phenylmaleimide irreversibly inhibits pyruvate transport into rat heart and liver mitochondria to a much greater extent than does N-ethylmaleimide, iodoacetate or bromopyruvate. alpha-Cyanocinnamate protects the pyruvate transporter from attack by this thiol-blocking reagent. 2. In both heart and liver mitochondria alpha-cyanocinnamate diminishes labelling by [3H]N-phenylmaleimide of a membrane protein of subunit mol.wt. 15000 on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. Exposure of mitochondrial to unlabelled N-phenylmaleimide in the presence of alpha-cyanocinnamate, followed by removal of alpha-cyanocinnamate and exposure to [3H]N-phenylmaleimide, produced specific labelling of the same protein. 4. Both labelling and kinetic experiments with inhibitors gave values for the approximate amount of carrier present in liver and heart mitochondria of 100 and 450 pmol/mg of mitochondrial protein respectively. 5. The turnover numbers for net pyruvate transport and pyruvate exchange at 0 degrees C were 6 and 200 min-1 respectively.

Erythrocyte membrane protein defects in hereditary spherocytosis patients in Turkish population

Hematology ◽  
2012 ◽  
Vol 17 (4) ◽  
pp. 232-236 ◽  
Author(s):  
Aylin Canbolat Ayhan ◽  
Inci Yildiz ◽  
Sedef Yüzbaşıoğlu ◽  
Tiraje Celkan ◽  
Hilmi Apak ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Hereditary Spherocytosis ◽  
Turkish Population ◽  
Erythrocyte Membrane Protein

scholarly journals Calcium-dependence of insulin receptor phosphorylation

1983 ◽  
Vol 214 (2) ◽  
pp. 361-366 ◽  
Author(s):  
W E Plehwe ◽  
P F Williams ◽  
I D Caterson ◽  
L C Harrison ◽  
J R Turtle
Keyword(s):  
Membrane Protein ◽  
Insulin Receptor ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Beta Subunit ◽  
Receptor Phosphorylation ◽  
32P Incorporation ◽  
Isolated Rat

Phosphorylation of the insulin receptor of isolated rat adipocytes in response to insulin has been studied. Immunoprecipitation of adipocyte membrane protein demonstrated increased incorporation of 32P after exposure to insulin for 15 min, but this was dependent on the presence of physiological concentrations of Ca2+ and Mg2+. Autoradiography of solubilized immunoprecipitated membrane protein after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that most of the 32P incorporation occurred in a band corresponding to Mr 95 000, which has been identified previously as the beta-subunit of the insulin receptor. 32P incorporation was inhibited by 2,4-dinitrophenol and trifluoperazine. It is suggested that insulin-receptor phosphorylation is an energy-requiring process that is Ca2+-dependent and may be modulated by calmodulin. Phosphorylation may proceed independently of glucose transport.

scholarly journals Some observations on the choice of detergent for solubilization of the human erythrocyte membrane

1977 ◽  
Vol 164 (2) ◽  
pp. 465-468 ◽  
Author(s):  
D A W Grant ◽  
S Hjertén
Keyword(s):  
Erythrocyte Membrane ◽  
Sodium Dodecyl Sulphate ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Human Erythrocyte Membrane ◽  
Ionic Detergents ◽  
Triton X

Solubilization of the human erythrocyte membrane by seven detergents is described. Components released into the supernatant or retained in the residue were identified by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Two non-ionic detergents exhibiting little u.v. absorption were more efficient than u.v.-absorbing Triton X-100. Evidence is presented of an interchange between protein PAS 1 and protein PAS 2.

Erythrocyte membrane protein alterations underlying clinical heterogeneity in hereditary spherocytosis

1994 ◽  
Vol 88 (1) ◽  
pp. 52-55 ◽  
Author(s):  
Emanuele Miraglla Giudice ◽  
Achille Iolascon ◽  
Luciano Pinto ◽  
Bruno Nobili ◽  
Silverio Perrotta
Keyword(s):  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Hereditary Spherocytosis ◽  
Clinical Heterogeneity ◽  
Erythrocyte Membrane Protein ◽  
Protein Alterations

Cyst Membrane Protein Composition as a Discriminant Character in the Genus Artemia. (International Study on Artemia LV)

1997 ◽  
Vol 77 (1) ◽  
pp. 265-268 ◽  
Author(s):  
T.J. Abatzopoulos ◽  
G.V. Triantaphyllidis ◽  
J.A. Beardmore ◽  
P. Sorgeloos
Keyword(s):  
Membrane Protein ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
International Study ◽  
Fibrous Layer ◽  
Cuticular Membrane ◽  
Cyst Membrane

Isolated embryonic membranes (i.e. the outer cuticular membrane, the fibrous layer, the inner cuticular membrane and the hatching membrane) and homogenates of incubated, decapsulated cysts of 16 populations from five Artemia species (Crustacea, Anostraca) were examined by sodium dodecyl-sulphate polyacrylamide gel electrophoresis. Characteristic differences in major polypeptides between 45 and 205 kD were seen. These differences might be used as markers for identification of different Artemia species. The validity of this approach in characterizing Artemia populations is discussed.

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