Get Analysis of Post-Translational Modifications and Proteolysis PDF

By Jennifer Elizabeth Grant, Hong Li

ISBN-10: 1493934708

ISBN-13: 9781493934706

This quantity highlights proteomics experiences of quantitative PTM alterations in either peripheral and significant apprehensive approach proteomes using the latest advances in mass spectrometry. Chapters contain sensible details touching on the basics of pattern instruction, liquid chromatography, and tandem mass spectrometry instrumental research and may elucidate top practices within the interpretation of knowledge utilizing glossy bioinformatics ways. Written for the preferred Neuromethods series, chapters comprise the type of aspect and key implementation recommendation that guarantees winning leads to the laboratory.

Authoritative and practical, Analysis of Post-Translational variations and Proteolysis in Neuroscience aims to ascertain winning ends up in the extra research of this important field.

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Harvest tissue. , western blots, IHC staining). Flash freeze the 50 mg samples directly in liquid nitrogen and transfer them into labeled cryo-vials. Store the tissue samples at À86  C. 2. Cut the remaining tissue (300–450 mg, wet weight) into small pieces and place into a round-bottom centrifuge tube. 3. Add 1 mL of freshly prepared urea lysis buffer for each 100 mg of wet tissue. 14 Hongbo Gu et al. 4. Homogenize the tissue sample using a Polytron set at maximum speed: 2 Â 20-s pulses. Chill on ice for 1 min between each pulse.

Freeze the eluate on dry ice (or À80  C freezer) for 2 h to overnight and lyophilize frozen peptide solution for a minimum of 2 days to assure that TFA has been removed from the peptide sample. 4. NOTE: The lyophilization should be performed in a standard lyophilization apparatus. DO NOT USE a SPEED-VAC apparatus at this stage of the protocol. 5. NOTE: The lysate digest may have a much higher volume than the 10 cc reservoir will hold (up to 50–60 mL from adherent cells) and therefore the peptides must be applied in several fractions.

Among all PTMs, ubiquitination and phosphorylation are the most highly represented in the identified proteins. Besides, large numbers of novel modification sites were identified on some crucial signaling nodes in neuronal pathways including mono-methyl-arginine in voltagedependent calcium channel (VGCC), lysine-succinylation on GABA transaminase, and mono-methyl-lysine on PAK (Fig. 6). Fig. 6 KEGG pathway analysis of identified proteins (pink rectangle) with PTMs in mouse brain. (a) Axon guidance, (b) GABAergic synapse.

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Analysis of Post-Translational Modifications and Proteolysis in Neuroscience by Jennifer Elizabeth Grant, Hong Li

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