Name: Proteomics of mouse liver microsomes: performance of different protein separation workflows for LC-MS/MS
Keywords: Not available

OmicsDI

Browse
Submit Data
Databases
API
Help

Dataset Information

266 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomics of mouse liver microsomes: performance of different protein separation workflows for LC-MS/MS

ABSTRACT: Not available

INSTRUMENT(S): instrument model, Agilent instrument model

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Liver

SUBMITTER: Victor Zgoda

PROVIDER: PRD000089 | Pride | 2009-07-28

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Proteomics of mouse liver microsomes: performance of different protein separation workflows for LC-MS/MS.

Zgoda Victor G VG Moshkovskii Sergei A SA Ponomarenko Elena A EA Andreewski Timofey V TV Kopylov Arthur T AT Tikhonova Olga V OV Melnik Stanislav A SA Lisitsa Andrei V AV Archakov Alexander I AI

Proteomics 20090801 16

The mouse liver microsome proteome was investigated using ion trap MS combined with three separation workflows including SDS-PAGE followed by reverse-phase LC of in-gel protein digestions (519 proteins identified); 2-D LC of protein digestion (1410 proteins); whole protein separation on mRP heat-stable column followed by 2-D LC of protein digestions from each fraction (3-D LC; 3703 proteins). The higher number of proteins identified in the workflow corresponded to the lesser percentage of run-to ...[more]

PMID: 19701918

Similar Datasets

Proteomic and bioinformatics analyses of mouse liver microsomes.

Project description: Not available

| S-EPMC3317213 | biostudies-literature

Rat Liver Microsomes by 2D-LC-MS/MS

Project description:Rat liver microsomes were analysed using offline strong cation exchange fractionation followed by reverse-phase chromatography coupled to quadrupole-time-of-flight high-resolution mass spectrometry using trypsin and pepsin parallel digestions. MS/MS files were searched against the UniProt protein database (release date 12-07-2011, 241 MB) by ProteinPilot software (version 4.1) using Paragon algorithm with the following parameters: Protein identification with thorough ID search effort, iodoacetamide for cysteine alkylation and no specified proteolytic enzyme, species set for rattus norvegicus with ID focus on biological modifications. Detection protein threshold of unused ProtScore > 0.05 (confidence > 10.0%) with false discovery rate (FDR) analysis. MS tolerance 0.05 Da on precursor ions and 0.1 Da on fragments. Search was performed for +2 to +4 charge states.

2013-02-19 | PXD000128 | Pride

Metabolism studies of paeoniflorin in rat liver microsomes by ultra-performance liquid chromatography coupled with hybrid quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF-MS/MS).

Project description: Not available

| S-EPMC6227959 | biostudies-literature

UPLC/MS MS data of testosterone metabolites in human and zebrafish liver microsomes and whole zebrafish larval microsomes.

Project description: Not available

| S-EPMC5847491 | biostudies-other

mouse liver microsomes phosphorylation with LC-MS/MS

Project description:The microsomes are re-formed vesicle-like artifacts, not ordinarily present in living cells, from pieces of the endoplasmic reticulum (ER), plasma membrane, mitochondria, and Golgi apparatus of broken eukaryotic cells. Typically, microsomes are separated by differential centrifuged from homogenized of cell or tissue. Based on enrichment of ER fractions, prepared microsomes mainly show a large of metabolic activity following high amount of metabolic enzyme, as cytochrome P450 (CYP). CYPs are important components of xenobiotic-metabolizing monooxygenase accounting for an approximate 75% of biotransformation of clinically relevant drugs. Hepatic CYP are ER-anchored hemoproteins involved in the metabolism of numerous endo- and xenobiotics including drugs, steroids, and carcinogens. The CYPs catalytic activity is subject to regulation via phosphorylation. In several previous studies, 8 CYP phosphorylation sites had been discovered in human. Protein kinase A (PKA) and protein kinase C (PKC) were identified as a major catalyst for the phosphorylation of CYPs in 2003. The phosphorylation of CYPs process to their ubiquitination undergoing ubiquitin-dependent 26S proteosomal degradation.

2017-04-04 | PXD003043 | Pride

mouse liver microsomes phosphorylation

2015-08-24 | PXD002221 | Pride

Dataset from proteomic analysis of rat, mouse, and human liver microsomes and S9 fractions.

Project description: Not available

| S-EPMC4510096 | biostudies-literature

The Metabolism of Separase Inhibitor Sepin-1 in Human, Mouse, and Rat Liver Microsomes.

Project description: Not available

| S-EPMC5949348 | biostudies-literature

Metabolic capabilities of cytochrome P450 enzymes in Chinese liver microsomes compared with those in Caucasian liver microsomes.

Project description: Not available

| S-EPMC3269586 | biostudies-literature