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Subject peptides

Step 3 Once formed the thiazolone derivative isomerizes to a more stable phenylthiohydantom (PTH) derivative which IS isolated and characterized thereby providing identification of the N terminal ammo acid The remainder of the peptide (formed m step 2) can be isolated and subjected to a second Edman degradation... [Pg.1134]

Only the N terminal amide bond is broken m the Edman degradation the rest of the peptide chain remains intact It can be isolated and subjected to a second Edman procedure to determine its new N terminus We can proceed along a peptide chain by beginning with the N terminus and determining each ammo acid m order The sequence is given directly by the structure of the PTH derivative formed m each successive degradation... [Pg.1135]

During the synthesis of peptides that contain 4-methoxybenzyl-protected cysteine residues, sulfoxide formation may occur. These sulfoxides, when treated with HF/ anisole, form thiophenyl ethers that cannot be deprotected therefore, the peptides should be subjected to a reduction step prior to deprotection. ... [Pg.282]

However, the use of a HPLC separation step enabled a remarkable acceleration of the deconvolution process. Instead of preparing all of the sublibraries, the c(Arg-Lys-O-Pro-O-P-Ala) library was fractionated on a semipreparative HPLC column and three fractions as shown in Fig. 3-2 were collected and subjected to amino acid analysis. According to the analysis, the least hydrophobic fraction, which eluted first, did not contain peptides that included valine, methionine, isoleucine, leucine, tyrosine, and phenylalanine residues and also did not exhibit any separation ability for the tested racemic amino acid derivatives (Table 3-1). [Pg.64]

The structures of these ylide polymers were determined and confirmed by IR and NMR spectra. These were the first stable sulfonium ylide polymers reported in the literature. They are very important for such industrial uses as ion-exchange resins, polymer supports, peptide synthesis, polymeric reagent, and polyelectrolytes. Also in 1977, Hass and Moreau [60] found that when poly(4-vinylpyridine) was quaternized with bromomalonamide, two polymeric quaternary salts resulted. These polyelectrolyte products were subjected to thermal decyana-tion at 7200°C to give isocyanic acid or its isomer, cyanic acid. The addition of base to the solution of polyelectro-lyte in water gave a yellow polymeric ylide. [Pg.378]

Schemes are available, however, that start from the free carboxylic acid, plus an activator . Dicyclohexylcarbodiimide, DCC, has been extensively employed as a promoter in esterification reactions, and in protein chemistry for peptide bond formation [187]. Although the reagent is toxic, and a stoichiometric concentration or more is necessary, this procedure is very useful, especially when a new derivative is targeted. The reaction usually proceeds at room temperature, is not subject to steric hindrance, and the conditions are mild, so that several types of functional groups can be employed, including acid-sensitive unsaturated acyl groups. In combination with 4-pyrrolidinonepyridine, this reagent has been employed for the preparation of long-chain fatty esters of cellulose from carboxylic acids, as depicted in Fig. 5 [166,185,188] ... Schemes are available, however, that start from the free carboxylic acid, plus an activator . Dicyclohexylcarbodiimide, DCC, has been extensively employed as a promoter in esterification reactions, and in protein chemistry for peptide bond formation [187]. Although the reagent is toxic, and a stoichiometric concentration or more is necessary, this procedure is very useful, especially when a new derivative is targeted. The reaction usually proceeds at room temperature, is not subject to steric hindrance, and the conditions are mild, so that several types of functional groups can be employed, including acid-sensitive unsaturated acyl groups. In combination with 4-pyrrolidinonepyridine, this reagent has been employed for the preparation of long-chain fatty esters of cellulose from carboxylic acids, as depicted in Fig. 5 [166,185,188] ...
A peptide, once released, is not subject to reuptake like most transmitters, but is broken down by membrane peptidases. There are no known peptide transporters so that reuptake and re-use are not likely. The peptidases are predominantly membrane bound at the synapse and many are metalloproteases in that they have a metal moiety, most often zinc, near the active site. These enzymes are generally selective for particular... [Pg.253]


See other pages where Subject peptides is mentioned: [Pg.65]    [Pg.93]    [Pg.85]    [Pg.65]    [Pg.93]    [Pg.85]    [Pg.164]    [Pg.1131]    [Pg.43]    [Pg.164]    [Pg.458]    [Pg.6]    [Pg.226]    [Pg.302]    [Pg.448]    [Pg.101]    [Pg.378]    [Pg.1131]    [Pg.119]    [Pg.141]    [Pg.554]    [Pg.1182]    [Pg.1190]    [Pg.855]    [Pg.863]    [Pg.109]    [Pg.84]    [Pg.15]    [Pg.8]    [Pg.96]    [Pg.110]    [Pg.198]    [Pg.233]    [Pg.33]    [Pg.136]    [Pg.142]    [Pg.45]    [Pg.151]    [Pg.540]    [Pg.581]    [Pg.286]    [Pg.495]    [Pg.97]    [Pg.28]   
See also in sourсe #XX -- [ Pg.176 ]




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Cumulative Subject peptides

Hydrolytic peptides Subject

Peptide bond stability Subject

Peptide synthesis General Subject

Peptides Subject index

Subject cyclic peptides)

Subject peptidic

Subject peptidic

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