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Amino acid analysis materials

Amino acid analysis, by reverse-phase HPLC, of acid-hydrolyzed uncross-linked recombinant resilin and cross-linked recombinant resilin clearly shows the presence of dityrosine in the cross-linked sample (Figure 9.3c). Further evidence of the presence of dityrosine was obtained by UV irradiation (Xmax,ex 315 nm Xmax,em 409 nm). Dityrosine endows natural resilin with pH-dependent blue fluorescence [38] on UV irradiation. The cross-linked recombinant resilin material was similarly fluorescent, strongly suggesting dityrosine cross-links. [Pg.259]

S.M. Halpine, Investigation of Artists Materials Using Amino Acid Analysis Introduction of the One Hour Extraction Procedure, Conservation Research, 51, 28 69 (1995). [Pg.255]

A study comprising five laboratories was carried out on the accuracy and precision of protein amino acid analysis. An important conclusion reached was that it is necessary to examine both accuracy and precision to achieve maximum improvement in either129. A commercially available single-cell protein, Pruteen, was proposed as reference material for the determination of amino acids and other substances in food. This recommendation was the result of a five-year-long study on the stability of this particular protein130. [Pg.1067]

The selectivity of different stationary phase materials can be applied using columns in sequence to provide high-speed isocratic separations instead of gradient elution. An example for amino acids analysis is shown later in Figure 4.15, where the same eluent was used for all of the separations and the fraction containing the sample components of interest was switched from one column to another. [Pg.17]

Boc-Cys-Tyr[Z(Br)]-Ile-Gln-Asn-Cys-Pro-Leu-Gly-MBHA-resin [prepared from the corresponding S-Fm-protected resin-linked peptide (50-60mg, 0.35mmol/g, 19 nmol) by treatment with piperidine/ DMF/[5-ME (10 10 0.7) at 25 °C for 3 h] was suspended in pH 8 buffered DMF (3 mL) in an open vessel at 25 °C for 1 h, washed, deblocked with TFA/CH2C12, and cleaved with HF/anisole (9 1) at 0 °C for 1 h to provide the crude peptide yield 16 xmol (88%). This material was purified by MPLC on a Lobar RP-8 column yield 8.5 xmol (53%) the product was characterized by amino acid analysis and HPLC. [Pg.112]

Recent approaches to the amino acid analysis of foods require maceration of the sample, hydrolysis of the proteins with HC1, and filtration. The resulting material may still include proteins (and fragmented peptides), carbohydrates, salts, urea, and lipids. The solution is then passed through a small column of cation exchanger (with a nominal cross-linking of at least 8%) in... [Pg.466]

JA White, RJ Hart, JC Fry. An evaluation of the Waters Pico-Tag system for the amino-acid analysis of food materials. J Auto Chem 8 170-177, 1986. [Pg.94]

CuBS4 has an apparent molecular mass of approximately 13 000 Da. Attempts to determine the amino acid analysis of this material have revealed that it contains very little amino nitrogen after performic acid oxidation, however, the sample was shown to contain abundant amino nitrogen. [Pg.10]

Protected Boc-Trp-Leu-Arg(Tos)-Lys[Z(2-a)]...Ala-Lys[Z(2-Cl)]-Ser(Bzl)-Gln-OBzl [23-84] (4.07 g, 0.4 mmol) was treated with TFA (30 mL) in an ice bath for 60 min. After removal of excess TEA, 5.7 M HCl in dioxane (0.14 mL, 0.8 mmol) was added and the product precipitated with Et20. The product was washed with Et20 and dried over NaOH pellets under reduced pressure. This material was dissolved together with Boc-Ser(Bzl)-Val-Ser(Bzl)-Glu(OBzl)...Glu(OBzl)-Arg(Tos)-Val-Glu(OBzl)-OH [1-22] (1.68 g, 0.48 mmol) in CHCI3/TFE (120 mL, 3 1), and then HODhbt (78 mg, 0.48 mmol) and 2 ( 0.09 mL, 0.48 mmol) were added. After stirring for 5h, the mixture was concentrated and chilled, excess aq 1% NaHCOs was added, and the precipitate was collected and washed with 1 M HCl and H2O. The product was dissolved in CHCI3/TFE (3 1) and after concentration, precipitated with MeCN. The precipitate was filtered off and washed with MeOH, EtOAc, and hexane to give the product yield 4.63 g (93%) amino acid analysis. [Pg.527]

Figure 3. Reverse phase HPLC of an in gel digest of 77 pmol of an unknown 135 kD protein. A. Chromatogram of the initial tryptic digest. Since there were few, if any probable peptide peaks not also present in the blank (panel B) and since amino acid analysis of the digested gel band indicated it still contained the protein, the gel band was washed twice with ISO /il 0.1 M Tris/HCl, pH 8, 50% CH3CN and digested again as described in Materials and Methods. Panel C shows the chromatogram that was obtained from this re-digest. Figure 3. Reverse phase HPLC of an in gel digest of 77 pmol of an unknown 135 kD protein. A. Chromatogram of the initial tryptic digest. Since there were few, if any probable peptide peaks not also present in the blank (panel B) and since amino acid analysis of the digested gel band indicated it still contained the protein, the gel band was washed twice with ISO /il 0.1 M Tris/HCl, pH 8, 50% CH3CN and digested again as described in Materials and Methods. Panel C shows the chromatogram that was obtained from this re-digest.
Amino acid analysis (AAA) is a classic analytical technique that characterizes proteins and peptides based on the composition of their constituent amino acids. It provides qualitative identification and is essential for the accurate quantification of proteinaceous materials. [Pg.124]

To 1.0 volume of serum or resin-treated urine, add 3.0 volumes of absolute ethanol in a centrifuge tube. Mix well and allow to stand for 10 minutes. Centrifuge any precipitated protein at 2000 rpm for 10 minutes. Decant off the ethanolic extract and add 3.0 volumes of chloroform. Mix well and allow to stand for 5 minutes. The aqueous layer on top of the chloroform-alcohol mixture contains the free amino acids and is pipetted into a separate tube. Aliquots of the extract of 0.10 ml and 0.20 ml are used for quantitative total amino acid analysis (Section 4.4). The remainder is evaporated to dryness in vacuo (40°) and the dried material is redissolved in 0.1 volume of water for use in spotting the plates for TLC amino acid analysis (Section 4.5). [Pg.160]

Data compiled from Plattner et al. (1977) and Tiggeman et al. (1981) have been normalized to reflect relative activities. Both studies reported the activity for MPOase(9), which is, therefore, taken as a reference. However, the activity of MPOase(9) is probably somewhat too high since it is based on pure material (i.e., without residual water or salt) as calculated from amino acid analysis, whereas the other data were obtained for weighed samples. MPOase(8), (9), and (11) correspond to microperoxidase with 8, 9, and 11 amino acids, respectively POase is horseradish peroxidase. [Pg.219]


See other pages where Amino acid analysis materials is mentioned: [Pg.57]    [Pg.335]    [Pg.4]    [Pg.155]    [Pg.231]    [Pg.207]    [Pg.204]    [Pg.14]    [Pg.52]    [Pg.53]    [Pg.116]    [Pg.785]    [Pg.709]    [Pg.285]    [Pg.33]    [Pg.10]    [Pg.19]    [Pg.28]    [Pg.109]    [Pg.285]    [Pg.163]    [Pg.31]    [Pg.147]    [Pg.191]    [Pg.208]    [Pg.685]    [Pg.82]    [Pg.249]    [Pg.14]    [Pg.66]    [Pg.959]    [Pg.222]    [Pg.15]    [Pg.258]   
See also in sourсe #XX -- [ Pg.186 , Pg.197 ]




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