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  • 4-thialaminine  (1)
  • DABITC: thin layer chromatography  (1)
  • Pectinesterase  (1)
  • Polypeptide expression  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Modification of tomato andAspergillus niger pectinesterases with diethyl pyrocarbonate (1996)
    Springer
    The protein journal 15 (1996), S. 127-130 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01887393
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    C-Terminal Sequence Determination of Modified Peptides by MALDI MS (1997)
    Springer
    The protein journal 16 (1997), S. 371-374 
    Details
    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
    URL: http://dx.doi.org/10.1023/A:1026328520307
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    By-products as an aid in residue identification during peptide sequence analysis with dimethylaminoazobenzene isothiocyanate (1982)
    Springer
    The protein journal 1 (1982), S. 257-262 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01025003
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of polypeptide expression in benign and malignant human breast lesions (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 582-587 
    Details
    ISSN: 0173-0835
    Keywords: Breast ; Tumor ; Two-dimensional polyacrylamide gel electrophoresis ; Polypeptide expression ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Results of two-dimensional electrophoresis (2-DE) analyses of human breast carcinoma are described. Tumor cells were extracted and purified from breast carcinomas with different proliferative indeces and degrees of genomic stability. Cells purified from fibroadenoma tissue served as controls for benign cells. The following results were observed: (i) Analysis of samples from different areas of the same tumor showed a high degree of similarity in the pattern of polypeptide expression. Similarly, analysis of two tumors and their metastases revealed similar 2-DE profiles. (ii) In contrast, large variations were observed between different lesions with comparable histological characteristics. Larger differences in polypeptide expression were observed between potentially highly malignant carcinomas compared to comparisons of less malignant lesions. These differences were in the same order of magnitude as those observed comparing a breast carcinoma to a lung carcinoma. (iii) The levels of all cytokeratin forms resolved (CK7, CK8, CK15, and CK18) were significantly lower in carcinomas compared to fibroadenomas. (iv) The levels of high molecular weight tropomyosins (1-3) were lower in carcinomas compared to fibroadenomas. The expression of tropomyosin-1 was found to be 1.7-fold higher in primary tumors with metastatic spread to axillar lymph nodes compared to primary tumors with no evidence of metastasis (p 〈 0.05). (v) The expression of proliferating cell nuclear antigen (PCNA) and some members of the stress protein family (pHSP60, HSP90, and calreticulin) were higher in carcinomas. We conclude that malignant progression of breast carcinomas results in large heterogeneity in polypeptide expression between different tumors, but that some common themes such as decreased expression of cytokeratin and tropomyosin polypeptides can be discerned.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180341
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    Paper (German National Licenses)
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