scholarly journals A Polymeric form of Haemoglobin-Binding Protein in Sheep Following Metabolic and Hormonal Disturbance

1972 ◽  
Vol 25 (5) ◽  
pp. 941 ◽  
Author(s):  
IG Jarrett
Keyword(s):  
Gel Electrophoresis ◽  
Binding Proteins ◽  
Serum Proteins ◽  
Binding Protein ◽  
Polymeric Form ◽  
Poly Acrylamide

The serum proteins of sheep have been examined by concave gradient poly-acrylamide gel electrophoresis. It would appear that sheep are usually lacking in haemoglobin-binding proteins (haptoglobins).

Properties of triiodothyronine-binding proteins in liver cytosol of rat

1983 ◽  
Vol 61 (9) ◽  
pp. 1035-1041 ◽  
Author(s):  
D. Bellabarba ◽  
S. Bédard ◽  
J. -G. Lehoux
Keyword(s):  
Gel Electrophoresis ◽  
Binding Proteins ◽  
Serum Proteins ◽  
Binding Protein ◽  
Gradient Centrifugation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sedimentation Coefficient ◽  
Gel Chromatography ◽  
Sucrose Density Gradient Centrifugation ◽  
Liver Cytosol

The electrophoretic mobility and the sedimentation coefficient were determined in partially purified preparations of both rat liver cytosol and serum triiodothyronine (T3)-binding proteins. Crude cytosol and serum, each labeled with [125I]T3, were filtered through a Sephadex G-100 column. The cytosol yielded a single T3-binding peak, whereas three binding components were recognized in the serum. Protamine sulfate precipitated the cytosol T3-binding protein, but had no effect on the serum T3-binders. The cytosol protein and the three binding proteins from serum were analyzed by polyacrylamide gel electrophoresis and sucrose density gradient centrifugation. The cytosol binder migrated as a single peak on gel electrophoresis with an Rf of 0.53, whereas the serum proteins had Rfs between 0.27–0.33. The sedimentation coefficient of the cytosol protein was 6.3 S, whereas it was 4.1 S for the major binding protein of the serum. These data indicate that: (i) preliminary purification by gel chromatography is a useful step for better characterization of the T3-binding proteins of the cytosol and serum; (ii) the cytosol binder is an acidic protein with completely different properties from those of the serum T3-binding proteins.

scholarly journals CONCANAVALIN A BINDING PROTEINS OF LYMPHOID CELL SURFACE

1974 ◽  
Vol 140 (2) ◽  
pp. 597-602 ◽  
Author(s):  
Yong Sung Choi ◽  
James C. Jenson
Keyword(s):  
Cell Surface ◽  
Affinity Chromatography ◽  
Concanavalin A ◽  
Lymphoid Cell ◽  
Gel Electrophoresis ◽  
Binding Proteins ◽  
Binding Protein ◽  
Lymphoid Cells

A Concanavalin A binding protein of chicken lymphoid cells was isolated by affinity chromatography of intact lymphoid cells. This protein with a mol wt of 160,000 daltons revealed two peptides (30,000 and 20,000 daltons) in SDS-acrylamide gel electrophoresis.

Differentiating various abnormalities of thyroxin binding to serum proteins by radioelectrophoresis of thyroxin and immunoassay of binding proteins

1990 ◽  
Vol 36 (3) ◽  
pp. 457-461 ◽  
Author(s):  
M R Pandian ◽  
C Morgan ◽  
J C Nelson ◽  
D A Fisher
Keyword(s):  
Binding Proteins ◽  
Serum Proteins ◽  
Binding Protein ◽  
Blue Staining ◽  
Bromphenol Blue ◽  
Relative Distribution ◽  
Agarose Gel Electrophoresis ◽  
Mass Ratio ◽  
Nonthyroidal Illness ◽  
Simple Method

Abstract Using the simple method of protein analysis described here, we could identify thyroxin (T4)-binding-protein abnormalities in euthyroid patients with hyperthyroxinemia or hypothyroxinemia. Serum incubated with [125I]thyroxin was analyzed by agarose gel electrophoresis, with bromphenol blue staining of protein. The relative distribution of radioactive T4 was determined for each binding protein--thyroxin-binding globulin (TBG), transthyretin, albumin, and T4-binding immunoglobulin (when present)--and the mass of T4 bound to each was determined. We also used sensitive immunoassays to quantify TBG, transthyretin, and albumin concentrations, then calculated the mass of T4 (as determined by electrophoresis) bound per unit mass of the respective binding protein. When the concentration of binding proteins was altered (e.g., TBG excess or TBG deficiency), the T4 binding/mass ratio for each protein remained within the expected range; but when the functional affinity of a binding protein was altered--as in dysalbuminemic hyperthyroxinemia and in low-T4 nonthyroidal illness--this ratio was abnormal. This procedure can be used to help identify TBG excess, TBG deficiency, dysalbuminemic hyperthyroxinemia, prealbumin-associated hyperthyroxinemia, variant TBG with reduced affinity for T4, euthyroid sickness, and T4-binding autoantibodies.

Small GTP-binding Protein RalA Associates with Weibel-Palade Bodies in Endothelial Cells

1999 ◽  
Vol 82 (09) ◽  
pp. 1177-1181 ◽  
Author(s):  
Hubert de Leeuw ◽  
Pauline Wijers-Koster ◽  
Jan van Mourik ◽  
Jan Voorberg
Keyword(s):  
Endothelial Cells ◽  
Binding Proteins ◽  
Binding Protein ◽  
Control Release ◽  
Small Gtpase ◽  
Gtp Binding Protein ◽  
Two Dimensional Gel Electrophoresis ◽  
Gtp Binding Proteins ◽  
Dense Granules ◽  
Gtp Binding

SummaryIn endothelial cells von Willebrand factor (vWF) and P-selectin are stored in dense granules, so-called Weibel-Palade bodies. Upon stimulation of endothelial cells with a variety of agents including thrombin, these organelles fuse with the plasma membrane and release their content. Small GTP-binding proteins have been shown to control release from intracellular storage pools in a number of cells. In this study we have investigated whether small GTP-binding proteins are associated with Weibel-Palade bodies. We isolated Weibel-Palade bodies by centrifugation on two consecutive density gradients of Percoll. The dense fraction in which these subcellular organelles were highly enriched, was analysed by SDS-PAGE followed by GTP overlay. A distinct band with an apparent molecular weight of 28,000 was observed. Two-dimensional gel electrophoresis followed by GTP overlay revealed the presence of a single small GTP-binding protein with an isoelectric point of 7.1. A monoclonal antibody directed against RalA showed reactivity with the small GTP-binding protein present in subcellular fractions that contain Weibel-Palade bodies. The small GTPase RalA was previously identified on dense granules of platelets and on synaptic vesicles in nerve terminals. Our observations suggest that RalA serves a role in regulated exocytosis of Weibel-Palade bodies in endothelial cells.

Rap1b Association with the Platelet Cytoskeleton Occurs in the Absence of Glycoproteins IIb/IIIa

1998 ◽  
Vol 79 (04) ◽  
pp. 832-836 ◽  
Author(s):  
Thomas Fischer ◽  
Christina Duffy ◽  
Gilbert White
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Binding Proteins ◽  
Binding Protein ◽  
Platelet Membrane ◽  
Low Molecular Weight ◽  
Membrane Glycoproteins ◽  
Gtp Binding Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

SummaryPlatelet membrane glycoproteins (GP) IIb/IIIa and rap1b, a 21 kDa GTP binding protein, associate with the triton-insoluble, activation-dependent platelet cytoskeleton with similar rates and divalent cation requirement. To examine the possibility that GPIIb/IIIa was required for rap1b association with the cytoskeleton, experiments were performed to determine if the two proteins were linked under various conditions. Chromatography of lysates from resting platelets on Sephacryl S-300 showed that GPIIb/IIIa and rap1b were well separated and distinct proteins. Immunoprecipitation of GPIIb/IIIa from lysates of resting platelets did not produce rap1b or other low molecular weight GTP binding proteins and immunoprecipitation of rap1b from lysates of resting platelets did not produce GPIIb/IIIa. Finally, rap1b was associated with the activation-dependent cytoskeleton of platelets from a patient with Glanzmann’s thrombasthenia who lacks surface expressed glycoproteins IIb and IIIa. Based on these findings, we conclude that no association between GPIIb/IIIa and rap1b is found in resting platelets and that rap1b association with the activation-dependent cytoskeleton is at least partly independent of GPIIb/IIIa.

scholarly journals The Interplay of RNA Binding Proteins, Oxidative Stress and Mitochondrial Dysfunction in ALS

Antioxidants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 552
Author(s):  
Jasmine Harley ◽  
Benjamin E. Clarke ◽  
Rickie Patani
Keyword(s):  
Oxidative Stress ◽  
Gene Expression ◽  
Mitochondrial Dysfunction ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Therapeutic Strategies ◽  
Lateral Sclerosis

RNA binding proteins fulfil a wide number of roles in gene expression. Multiple mechanisms of RNA binding protein dysregulation have been implicated in the pathomechanisms of several neurodegenerative diseases including amyotrophic lateral sclerosis (ALS). Oxidative stress and mitochondrial dysfunction also play important roles in these diseases. In this review, we highlight the mechanistic interplay between RNA binding protein dysregulation, oxidative stress and mitochondrial dysfunction in ALS. We also discuss different potential therapeutic strategies targeting these pathways.

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