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  • 1995-1999  (2)
  • 1985-1989  (1)
  • Biochemistry and Biotechnology  (1)
  • N-terminal processing  (1)
  • Pectinesterase  (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
    Expression inEscherichia coli of active human alcohol dehydrogenase lacking N-terminal acetylation (1987)
    Springer
    Bioscience reports 7 (1987), S. 969-974 
    Details
    ISSN: 1573-4935
    Keywords: alcohol dehydrogenase ; expression plasmid ; immunodetection ; N-terminal processing ; E. coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Human alcohol dehydrogenase (ADH, tiff isozyme of class I) was expressed in Escherichia coli, purified to homogeneity, and characterized regarding N-terminal processing. The expression system was obtained by ligation of a cDNA fragment corresponding to the fl-subunit of human liver alcohol dehydrogenase into the vector pKK 223-3 containing the tac promoter. The enzyme, detected by Western-blot analysis and ethanol oxidizing activity, constituted up to 3 ~o of the total amount of protein. Recombinant ADH was separated from E. coli ADH by ion-exchange chromatography and the isolated enzyme was essentially pure as judged by SDS-polyacrylamide gel electrophoresis and sequence analysis. The N-terminal sequence was identical to that of the authentic fl-subunit except that the N-terminus was non-acetylated, indicating a correct removal of the initiator methionine, but lack of further processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01122131
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    Paper (German National Licenses)
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  • 3
    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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