Read e-book online A Practical Guide to Protein and Peptide Purification for PDF

By Paul T. Matsudaira

ISBN-10: 0124802826

ISBN-13: 9780124802827

Why a moment Edition?
The moment variation offers useful solutions to the final query, ''How am i able to receive priceless series info from my protein or peptide?'' instead of the extra particular query requested within the first version, ''How am i able to receive the N-terminal sequence?'' very important new tools contain methods of facing blocked N termini, machine research of protein sequences, and the new revolution in mass spectrometry.

Key Features
Highlights of the second one Edition:
* Mass spectrophotometric characterization of proteins and peptides
* N-terminal sequencing of proteins with blocked N termini
* inner amino acid series research after protease digestion in-gel and on-blot
* superior microscale peptide purification methods
* desktop research of protein sequences
* New protocols confirmed and sophisticated via daily use in authors' laboratories
* up-to-date reference bankruptcy overlaying all features of protein microsequencing

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Extra info for A Practical Guide to Protein and Peptide Purification for Microsequencing

Sample text

However, this type of pattern may also result from an impure starting sample. Scanning the data for the presence of sequence motifs or patterns (see below) may also provide evidence regarding a possible homology since consensus sequences are thought to be a characteristic of specific protein families. Information about the chemical and functional properties of the sample being studied provides valuable insight that can often indicate whether a potential structural relationship merits further consideration.

Electroblotting is preferred over electroelution because fewer manipulations are required. With current electroblotting protocols, N-terminal sequence is usually obtained from the electrophoresis of approximately 1 0 - 1 0 0 pmol of protein. N-terminal sequence analysis of high-molecular-weight proteins (>100 kDa) presents special problems. Proteins of this size are more difficult to electrophorese out of a gel and are usually not amenable to strategies based on SDS-PAGE. High-molecular-weight samples are usually loaded directly into the sequenator, but they must be purified and exchanged into appropriate solvents using standard procedures which generally require larger quantities of starting sample.

The most reliable quantitation method is from amino acid analysis. Other methods include micro-Lowry, BCA, or dye-binding assays, estimation from silver stain or Coomassie blue-stained gels, enzyme or antibody assays, or absorbance. The later methods are less accurate, especially in the low microgram amounts. 13 This page intentionally left blank 1 Strategies for Obtaining Partial Amino Acid Sequence Data from Small Quantities (<500 pmol) of Pure or Partially Purified Protein Harry Charbonneau Department of Biochemistry Purdue University West Lafayette, Indiana Requirements for Protein Sequence Analysis Purification Strategies N-Terminal Analysis Complete Fragmentation Complete Fragmentation of Proteins Purified by SDS-Gel Electrophoresis Limited Proteolysis Computer Analysis of Protein Sequences S e q u e n c e A n a l y s i s Software A n a l y z i n g Database Searches Conducted with Partial S e q u e n c e Data D e t e c t i n g S e q u e n c e Patterns or Motifs D e s i g n i n g O l i g o n u c l e o t i d e Probes, P C R Primers, and Synthetic Peptide A n t i g e n s A Practical Guide to Protein and Peptide Purification for Microsequencing, Second Edition Copyright © 1993 by Academic Press, Inc.

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A Practical Guide to Protein and Peptide Purification for Microsequencing by Paul T. Matsudaira

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