A differential protein solubility approach for the depletion of highly abundant proteins in plasma using ammonium sulfate

The Analyst ◽  
2015 ◽  
Vol 140 (24) ◽  
pp. 8109-8117 ◽  
Author(s):  
Ravi Chand Bollineni ◽  
Ingrid J. Guldvik ◽  
Henrik Grönberg ◽  
Fredrik Wiklund ◽  
Ian G. Mills ◽  
...  
Keyword(s):  
Ammonium Sulfate ◽  
Proteomic Analysis ◽  
Protein Solubility ◽  
Plasma Samples ◽  
Differential Protein ◽  
Saturated Ammonium Sulfate ◽  
Sulfate Solutions

This work reports a precipitation and differential protein solubility approach using saturated ammonium sulfate solutions as a depletion and fractionation approach for shotgun proteomic analysis of plasma samples.

scholarly journals PURIFICATION OF THROMBIN

1942 ◽  
Vol 25 (5) ◽  
pp. 679-687 ◽  
Author(s):  
H. Milstone
Keyword(s):  
Ammonium Sulfate ◽  
Specific Activity ◽  
Saturated Ammonium Sulfate ◽  
Sulfate Solutions ◽  
Ionic Calcium

1. Under certain conditions crude prothrombin changes to thrombin without the addition of extraneous activators and in the absence of ionic calcium. 2. Thrombin is soluble in 0.45 saturated ammonium sulfate, whereas crude prothrombin is not. 3. Partially purified thrombin is comparatively stable in concentrated ammonium sulfate solutions at pH 5.2. 4. A method based on the above facts yields a thrombin preparation the specific activity of which is 100 to 175 times the potential specific activity of whole plasma.

Thermodynamic and Transport Properties of Some Disaccharides in Aqueous Ammonium Sulfate Solutions at Various Temperatures

2008 ◽  
Vol 53 (8) ◽  
pp. 1713-1724 ◽  
Author(s):  
Parampaul K. Banipal ◽  
Vickramjeet Singh ◽  
Gurpreet Kaur ◽  
Mandeep Kaur ◽  
Tarlok S. Banipal
Keyword(s):  
Transport Properties ◽  
Ammonium Sulfate ◽  
Sulfate Solutions ◽  
Thermodynamic And Transport Properties

MECHANISMS OF PLATELET AGGREGATION BY ACIDIC MUCOPOLYSACCHARIDE EXTRACTED FROM STICHOPUS JAPONICUS SELENKA IN HUMANS AND RABBITS

1987 ◽  
Author(s):  
J Z Li ◽  
E C-Y Lian
Keyword(s):  
Platelet Aggregation ◽  
Ammonium Sulfate ◽  
Human Platelets ◽  
Platelet Inhibitors ◽  
Rabbit Plasma ◽  
Human Fibrinogen ◽  
Stichopus Japonicus ◽  
Saturated Ammonium Sulfate ◽  
Rabbit Platelets ◽  
Induced Aggregation

It has been reported that acidic mucopolysaccharide extracted from sea cucumber (Stichopus japonicus selenka) (SJAMP) induced the aggregation of human and animal platelets by an unknown mechanism, using platelet-rich plasma (prp) and washed human and rabbit platelets we studied the effects of storage, platelet inhibitors, and various plasmas and their fractions on SJAMP-induced platelet aggregation. we found that the lowest concentrations of SJAMP required for aggregation of human and rabbit platelets were 0.4 and 2 ug/ml respectively. The reactivity of human platelets to SJAMP decreased with time after drawing of blood; rabbit platelets did not show this phenomenon. Platelet inhibitors such as aspirin, indomethacin, apyrase, antimycin, 2-deoxy-D-glucose, and EDTA inhibited by 50 to 100% the aggregation of human platelets induced by SJAMP; but these inhibitors had no effect on SJAMP-induced aggregation of rabbit platelets. Washed human and rabbit platelets were not aggregated by SJAMP. The aggregation of washed human platelets by SJAMP was restored completely by human or rabbit plasma, by human fibrinogen, or by 0 to 30% saturated ammonium sulfate fraction but not by serum. The aggregation of rabbit platelets by SJAMP could only be restored by rabbit plasma or serum, or by 50 to 60% saturated ammonium sulfate fraction. The data indicate that the mechanisms of aggregation of human and rabbit platelets by SJAMP are different. THe SJAMP-induced human platelet aggregation is dependent upon metabolism, release of ADP and the cyclooxygenase pathway requiring fibrinogen and Ca++. The aggregation of rabbit platelets induced by SJAMP is independent of metabolism, release of ADP and cyclooxygenase pathway, and does not require fibrinogen and Ca++, but needs certain protein(s) in the 50 to 60% saturated ammonium sulfate fraction of rabbit plasma.

Glyoxal in Aqueous Ammonium Sulfate Solutions: Products, Kinetics and Hydration Effects

2011 ◽  
Vol 45 (15) ◽  
pp. 6336-6342 ◽  
Author(s):  
Ge Yu ◽  
Amanda R. Bayer ◽  
Melissa M. Galloway ◽  
Kyle J. Korshavn ◽  
Charles G. Fry ◽  
...  
Keyword(s):  
Ammonium Sulfate ◽  
Sulfate Solutions

Proteomic analysis of differential protein expression in human atherosclerotic plaque progression

2005 ◽  
Vol 206 (1) ◽  
pp. 39-45 ◽  
Author(s):  
Marjo MPC Donners ◽  
Monique J Verluyten ◽  
Freek G Bouwman ◽  
Edwin CM Mariman ◽  
Bart Devreese ◽  
...  
Keyword(s):  
Protein Expression ◽  
Atherosclerotic Plaque ◽  
Proteomic Analysis ◽  
Plaque Progression ◽  
Differential Protein Expression ◽  
Human Atherosclerotic Plaque ◽  
Differential Protein

Proteomic analysis of lung biopsies: Differential protein expression profile between peritumoral and tumoral tissue

PROTEOMICS ◽  
2004 ◽  
Vol 4 (2) ◽  
pp. 442-447 ◽  
Author(s):  
Patricia Alfonso ◽  
Myriam Catalá ◽  
María Luisa Rico-Morales ◽  
Gonzalo Durante-Rodríguez ◽  
Ernesto Moro-Rodríguez ◽  
...  
Keyword(s):  
Protein Expression ◽  
Expression Profile ◽  
Proteomic Analysis ◽  
Protein Expression Profile ◽  
Differential Protein Expression ◽  
Differential Protein ◽  
Lung Biopsies

SELDI-TOF-Based Proteomic Analysis of Plasma Samples as a Diagnostic Tool to Predict Acute Graft-Versus-Host Disease after Allogeneic Stem Cell Transplantation

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 1165-1165
Author(s):  
Vanessa Wittke ◽  
Harald Binder ◽  
Stefan Zimmermann ◽  
Dietmar Pfeifer ◽  
Martin Schumacher ◽  
...  
Keyword(s):  
Stem Cell ◽  
Stem Cell Transplantation ◽  
Cell Transplantation ◽  
Plasma Protein ◽  
Graft Versus Host Disease ◽  
Diagnostic Tool ◽  
Proteomic Analysis ◽  
Plasma Samples ◽  
Host Disease ◽  
Graft Versus Host

Abstract Allogeneic hematopoietic stem cell transplantation (SCT) offers a curative treatment option for high-risk hematological tumors. Graft-versus-host disease (GvHD) is a severe and potentially life-threatening complication of allogeneic SCT. GvHD is caused by the activation of transplanted alloreactive T-cells and results in severe inflammation of host tissues in skin, liver, and gastrointestinal tract. Manifest GvHD can be diagnosed by clinical criteria and histology only. So far, no diagnostic blood test is able to detect imminent GvHD. GvHD is prevented and treated by systemic immunosuppression which is associated with opportunistic infections and higher relapse rates. Therefore, reliable detection of incipient GvHD would allow to investigate preemptive immunosuppressive therapy tailored to individual patients at appropriate time points. Proteomic profiling is based on the premise that alterations related to pathological states (e.g., GvHD) are accompanied by quantitative and qualitative alterations in plasma protein profiles. The surface-enhanced laser desorption/ionization (SELDI) technology relies on time-of-flight mass spectrometry for accurate measurement of the mass-to-charge ratio (m/z) of proteins that have been preselected on appropriate functional surfaces. We conducted a prospective case-control study based on >3000 serial plasma samples of 236 consecutive patients undergoing allogeneic SCT. 43 patients developed acute GvHD grade I-IV during their sampling period and were matched to control patients remaining GvHD-free. Matching criteria were prior antithymocyte globulin treatment, donor type (related versus unrelated), conditioning protocol, remission status at SCT, diagnosis, age, and sex. These factors were ranked in the listed order. Plasma protein patterns were obtained by SELDI-TOF on day -2 prior to the onset of clinical GvHD and compared to 43 plasma samples obtained on the corresponding day after SCT from the matched GvHD-free patients. In order to enhance the number of analyzable proteins, plasma samples were fractionated to yield 5 different sets of SELDI spectra. Protein peak positions and calibrated peak heights were determined according to Yasui et al (J Biomed Biotechnol, 2003). To identify a limited number of predictive peaks, a sparse logistic regression model was fitted by a boosting approach (Tutz & Binder, Computational Statistics & Data Analysis, 2007), resulting in 4 peaks at 11963, 22363, 22479, and 30977 Da. Prediction performance of a signature derived from this approach on new data was evaluated using bootstrap samples, resulting in an estimated misclassification rate of 38.5%, an estimated sensitivity of 61.0%, and specificity of 60.5% In addition, the identified predictive peaks could be recovered in most bootstrap samples, indicating sufficient stability of the signature. While the performance of this assay strategy is insufficient for use in clinical practice at present, our data nevertheless demonstrate the potential of proteomic plasma analysis in combination with a tailored statistical analysis to identify GvHD prior to its clinically recognizable onset. In contrast to the clinical routine of immunosuppressive GvHD prophylaxis for all patients after allogeneic SCT with treatment escalation in the case of clinically relevant GvHD, this diagnostic tool therefore offers the perspective for preemptive GvHD therapy administered only to patients with an imminent GvH reaction. Such a tailored GvHD strategy may represent a cornerstone to reduce the risk of infectious complications and tumor relapse while maintaining effective GvHD control in patients at risk. Current work addresses the identity of the index peaks, the temporal evolution of the signature, and refinement of the proteomic analysis.

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