Comprehensive proteome analysis of mouse liver by ampholyte-free liquid-phase isoelectric focusing

2008 ◽  
Vol 29 (11) ◽  
pp. 2372-2380 ◽  
Author(s):  
Hua Zhong ◽  
Dong Yun ◽  
Chen Zhang ◽  
Pengyuan Yang ◽  
Huizhi Fan ◽  
...  
Keyword(s):  
Liquid Phase ◽  
Isoelectric Focusing ◽  
Mouse Liver ◽  
Proteome Analysis

scholarly journals Fractionation of chicken egg proteome by isoelectric point in liquid phase

2014 ◽  
pp. 39-42
Author(s):  
Gabriella Gulyás ◽  
András Jávor ◽  
Tünde Radócz ◽  
Ádám Simon ◽  
Levente Czeglédi
Keyword(s):  
Liquid Phase ◽  
Isoelectric Point ◽  
Proteome Analysis ◽  
Egg Yolk ◽  
Animal Science ◽  
Complex Protein ◽  
Sample Purification ◽  
Protein Discovery ◽  
Optimisation Procedure ◽  
Proteomic Methods

The application of proteomics is relevant to physiology, reproduction, immunology, muscle and lactational biology in animal science, altough its use is still limited. One of the greatest challenges of proteome analysis is the reproducible fractionation of the complex protein mixtures. The fractionation methods can increase the probability of biomarker protein discovery. The fractionation by liquid-phase isoelectric focusing is one of the prefractionation methods. As a result, protein fractions can be easily collected, pooled and refractionated. There is a lack in the knowledge of gel-based proteomic methods of egg as only a limited number of protocols can be found in the literature, thus sample purification and fractionation require a time consuming optimisation procedure. The aim of this study was to fractionate egg yolk and white proteins by isoelectric point in liquid phase.

Liquid-phase isoelectric focusing of cardiac proteins: differential separation of cMyBP-C phosphorylation states

2007 ◽  
Vol 42 (6) ◽  
pp. S241-S242
Author(s):  
K.R. Sultan ◽  
L. Pohlmann ◽  
D. Juhr ◽  
T. Eschenhagen ◽  
L. Carrier
Keyword(s):  
Liquid Phase ◽  
Isoelectric Focusing

scholarly journals Antibody-affinity purification of novel α-l-fucosidase from mouse liver

1987 ◽  
Vol 245 (2) ◽  
pp. 589-593 ◽  
Author(s):  
L D Laury-Kleintop ◽  
I Damjanov ◽  
J A Alhadeff
Keyword(s):  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Human Liver ◽  
Mouse Liver ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Antibody Affinity ◽  
Native Polyacrylamide Gel Electrophoresis ◽  
Sepharose 4B

Previous studies have documented the presence of a novel alpha-L-fucosidase in mouse liver that contains unique basic isoelectric forms and that is antigenically similar to, but not identical with, human liver alpha-L-fucosidase [Laury-Kleintop, Damjanov & Alhadeff (1985) Biochem. J. 230, 75-82]. In the present investigation, mouse liver alpha-L-fucosidase was purified approx. 26,500-fold in 10% overall yield by antibody-affinity chromatography with the IgG fraction of goat anti-(human alpha-L-fucosidase) antibody coupled to Sepharose 4B. Native polyacrylamide-gel electrophoresis and SDS/polyacrylamide-gel electrophoresis indicated that the mouse fucosidase is highly purified if not homogeneous. Isoelectric focusing demonstrated that all enzymic forms found in crude mouse liver supernatant fluids were purified by the antibody-affinity procedure.

scholarly journals Technical Hurdles When Applying Isoelectric Focusing to Membrane Proteome Analysis

2008 ◽  
Vol S2 (01) ◽  
pp. 141-142
Author(s):  
T. C.W. Poon ◽  
N. Liu ◽  
H. W.C. Leung ◽  
E. C.H. Yip ◽  
Z. Cai
Keyword(s):  
Isoelectric Focusing ◽  
Proteome Analysis ◽  
Membrane Proteome

scholarly journals Proteomic analysis of subarachnoid hemorrhage - liquid phase isoelectric focusing in complex protein sample

2016 ◽  
Vol 85 (3) ◽  
pp. 161
Author(s):  
Joanna Hajduk ◽  
Bartosz Sokół ◽  
Agata Swiatly ◽  
Jan Matysiak ◽  
Piotr Nowicki ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Subarachnoid Hemorrhage ◽  
Liquid Phase ◽  
Isoelectric Focusing ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Proteomic Approach ◽  
Intersection Analysis ◽  
New Perspective ◽  
Tof Ms

Background: The aim of this study was to present the proteomic approach based on liquid phase isoelectric focusing fractionation coupled to nLC-MALDI-TOF/TOF-MS/MS analysis to characterize cerebrospinal fluid from control patients and those suffering from subarachnoid hemorrhage. The new perspective in characterization of this brain neuropathology are in constant demand to point a valuable panel of indicators which could improve the treatment outcome.Methods: The cerebrospinal fluid samples were applied to a commercial liquid phase isoelectric focusing apparatus and separated into 10 fractions by pI. Further, the untargeted mass spectrometry investigations were performed with data dependent acquisition mode for full-scan MS analysis with subsequently MS/MS fragmentation by using nLC-MALDI-TOF/TOF-MS/MS.Results: In total, the detection of 1664 and 2187 unique tryptic peptides provided biological evidence for 134 and 271 proteins in control and subarachnoid hemorrhage sample, respectively. The interpretation of liquid phase separation was performed by intersection analysis of two items between groups of ten fractions. The cumulative intersection exploration revealed the highest concentration of the detected components in the middle fractions of the focusing chamber, whereas the gradual dilution appeared on its extreme.Conclusions: The employed strategy ensured overall screening of investigated material presenting the proteins abundance in the current state of analysis. Few proteins such as proenkephalin A, peroxiredoxin-6, cathepsin B, thrombospondin-1, glial fibrillary acidic protein and α – spectrin were recognized as potential indicators, according to literature, pointing the possibility for its monitoring in further studies as panel of valuable biomarkers. 

Proteome Analysis of Mouse Liver Microsomal Fraction Using 2D BN/SDS-PAGE

2008 ◽  
Vol S2 (01) ◽  
pp. 118-118
Author(s):  
H. Saledekh ◽  
F. Shekari ◽  
B. Jordan ◽  
H. Baharvand
Keyword(s):  
Mouse Liver ◽  
Microsomal Fraction ◽  
Proteome Analysis ◽  
Sds Page ◽  
Liver Microsomal Fraction
Sign in / Sign up

Export Citation Format

Share Document