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  • 4-thialaminine  (1)
  • DABITC: thin layer chromatography  (1)
  • Pectinesterase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 15 (1996), S. 127-130 
    ISSN: 1573-4943
    Keywords: Pectinesterase ; tomato ; Aspergillus niger ; histidine modification ; diethyl pyrocarbonate ; inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The role of histidine residues in pectinesterases was evaluated by monitoring the sensitivity to modification with diethyl pyrocarbonate in the tomato andAspergillus niger enzymes. Different and incomplete losses of enzyme activity were obtained. Inactivation of the enzymes was proportional to the histidine content (two in the tomato T1 form, six in theAspergillus form), suggesting that accessible histidine residues do not have active-site functions in these pectinesterases, but contribute to the overall structural stability. Lack of His roles in common between the enzyme forms is in agreement with the structures of pectinesterases having no conserved His residues.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 16 (1997), S. 371-374 
    ISSN: 1573-4943
    Keywords: MALDI mass spectrometry ; carboxypeptidases ; chemical modification ; homoarginine ; 4-thialaminine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Peptides, cleaved by a mixture of carboxypeptidases CPP and CPY, can be detected by MALDI MS and the amino acid sequence thereby determined by calculation of the differences between consecutive peaks. In the present study we have used derivatizations of Lys and Cys to facilitate identification of these residues. Since the mass values do not readily distinguish Lys from Gln, we have converted Lys to homoarginine by guanidination, allowing simple detection of Lys. To identify the Cys positions in peptides that contain cystine, cysteic acid, or carboxymethylcysteine is not possible using CPY and CPP because of the lack of proteolytic cleavage. Instead we find that identification of Cys residues within the sequence can be achieved after conversion to a basic derivative, 4-thialaminine (Thi), by trimethylaminoethylation.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4943
    Keywords: DABITC: thin layer chromatography ; sequence identification and thiohydantoin by-products
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract 4-N,N-Dimethylaminoazobenzene 4′-isothiocyanate degradations permit sensitive and fast manual sequence analysis, but assignments of some residues are difficult. Hydrophobic residues, especially leucine and isoleucine, are badly resolved on polyamide thin-layer chromatography. Differently colored by-products have been described before for a few labile residues, but it is now shown that most residues can give rise to characteristic by-products. These have different colors and chromatographic properties, depending on the nature of the parent residue. Thus, two to three sets of spots characterize each residue, giving multiple identification with increased reliability. Although variable and dependent on chemicals and conditions, by-products are often prominent after conversion with 50% trifluoroacetic acid, and can be utilized to improve the identifications.
    Type of Medium: Electronic Resource
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