Titlebook: Methods in Protein Sequence Analysis; Kazutomo Imahori,Fumio Sakiyama Book 1993 Springer Science+Business Media New York 1993 Amino acid.P

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Capillary Liquid Chromatography: A Tool for Protein Structural Analysisisolation of proteins and peptides for the purpose of structural analysis. It is also the method of choice for the identification and quantitation of phenylthiohydantoin (PTH) derivatives, the products of the Edman degradation procedure employed for amino acid sequence analysis. The major advantage

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Capillary Electrophoresis in Structural Characterization of Polypeptides1989). These features make the technique attractive also for preparative attempts in structural analyses, but the small volumes (nl) and the correspondingly small amounts (fmol) have long been considered a difficulty in preparative applications. However, recently we showed that capillary zone electr

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Sensitization of Gas-Phase Protein Sequencer using Fluorescein Isothiocyanate (FITC)proteins (Hewick ., 1981). Further sensitization of sequence analysis has become one of the most important targets together with the development of micropurification methods and blotting technology with two dimensional gel electrophoresis. For sensitive detection of the amino acid derivatives result

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Thiobenzoylation Method of Protein Sequencing: Gas Chromatography/Mass Spectrometric Detection of 5- method attracted limited interest but facilitated the subsequent development of the closely-related thioacetylation method (Doolittle ., 1977), wherein the 2-methyl-5(4.)-thiazolone cleavage product is identified by back-hydrolysis to the parent amino acid. The 2-methyl-5(4.)-thiazolone is a volati

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Deblocking and Subsequent Microsequence Analysis of ,-Terminally Blocked Proteins Immobilized on PVDluoride (PVDF) membrane can be easily sequenced by a gas-phase sequencer (Matsudaira, 1987). However, even if the proteins are successfully separated by PAGE and electroblotted onto PVDF membrane, the .-terminal amino acid sequences of proteins with a blocking group at the .-terminus cannot be deter

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Development of Novel C-Terminal Sequencing Methodsl process, confirming recombinant proteins and cloning. Carboxypeptidase digestion has been commonly used with limitations. Since a classical isothiocyanate degradation was proposed, several modifications were reported in the past two conferences (Hawkes and Boyd, 1991; Inglis ., 1991; Miller and Sh

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A New Chemical Approach to C-Terminal Microsequence Analysis via the Thiohydantoindes and proteins. With the exception of proline, all amino acids that might have been expected to give difficulties were shown to be degraded normally in peptides (Inglis ., 1989; Inglis ., 1990). These findings have been largely corroborated by others (Bailey ., 1992) using different reaction condi