✦ LIBER ✦

Improved instrumentation for large-size two-dimensional protein maps

✍ Scribed by Renato Millioni; Manuela Miuzzo; Lucia Puricelli; Elisabetta Iori; Stefano Sbrignadello; Ryan Dosselli; Daniela Cecconi; Paolo Tessari; Pier Giorgio Righetti

Publisher: John Wiley and Sons
Year: 2010
Tongue: English
Weight: 127 KB
Volume: 31
Category: Article
ISSN: 0173-0835
DOI: 10.1002/elps.201000460

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Novel instrumentation for performing large‐size (>25 cm) 2‐D maps is reported here. To perform the first dimension, we developed a power supply that can deliver a voltage of up to 15 000 V and allows regulation of current (up to 200 μA) onto each individual focusing IPG strip. The IEF strip tray can accommodate up to 12 IPG strips and the electrodes slide on a ruler, thus permitting running strips of any length up to 45 cm. In addition, this apparatus also includes a second power supply that allows the performance of electrophoresis at high amperage (400 mA) and a Peltier system that allows a 10–80°C temperature control.

📜 SIMILAR VOLUMES

Human proteome enhancement: High-recover

Human proteome enhancement: High-recovery method and improved two-dimensional map of colostral fat globule membrane proteins

✍ Stefania Quaranta; Maria Gabriella Giuffrida; Maria Cavaletto; Carlo Giunta; Jas 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 105 KB

A modification for the improved analysis

A modification for the improved analysis of differential protein accumulation by two-dimensional polyacrylamide gel electrophoresis

✍ Abul K. M. Ekramoddoullah; Yingchun Tan 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 93 KB 👁 3 views

Phenolic compounds present in conifer tissues interfere with the analysis of conifer proteins by twodimensional (2-D) gel electrophoresis, causing gel streaking and distortion of protein patterns. A protocol was established by modifying the Hochstrasser method and using the Millipore 2 D Investigato

Using size exclusion chromatography-RPLC

Using size exclusion chromatography-RPLC and RPLC-CIEF as two-dimensional separation strategies for protein profiling

✍ David C. Simpson; Seonghee Ahn; Ljiljana Pasa-Tolic; Bogdan Bogdanov; Heather M. 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 386 KB

Improved method for identification of pr

Improved method for identification of proteins using two-dimensional electrophoresis with immobilized pH gradient isoelectric focusing

✍ Dr. Robert B. Mackin; Veronica A. Raker; Joachim Spiess 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 360 KB 👁 1 views

Recent advances in protein sequence analysis now permit the determination of partial N-terminal and internal primary structure from low picomole quantities of protein. The major remaining hurdles to sequence analysis of small amounts of protein are the identification, isolation, and handling of micr

Alkylation kinetics of proteins in prepa

Alkylation kinetics of proteins in preparation for two-dimensional maps: A matrix assisted laser desorption/ionization-mass spectrometry investigation

✍ Marina Galvani; Mahmoud Hamdan; Ben Herbert; Pier Giorgio Righetti 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 347 KB 👁 2 views

Two-dimensional separation system by on-

Two-dimensional separation system by on-line hyphenation of capillary isoelectric focusing with pressurized capillary electrochromatography for peptide and protein mapping

✍ Juan Wei; Xue Gu; Yan Wang; Yi Wu; Chao Yan 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 284 KB 👁 2 views

A novel on-line 2-D system was developed for peptide and protein mapping. The system combines capillary IEF (cIEF) with pressurized CEC (pCEC) using a micro-injection valve as the interface. Sample fractions, which were focused and separated in the firstdimension cIEF based on their differences in p