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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of latex allergenic components by capillary zone electrophoresis and N-terminal sequence analysis (1998)
    Springer
    Journal of biomedical science 5 (1998), S. 421-427 
    Details
    ISSN: 1423-0127
    Keywords: Latex ; Capillary zone electrophoresis ; Sequence ; Hevein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In a previous study, protein components purified from latex gloves that elicited allergenic reactions were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and yielded apparent molecular weights of 14, 22, 30, 34, 46, and 58 kD. These allergenic components were isolated for further characterization by capillary zone electrophoresis and N-terminal amino acid sequence analysis. These components all migrated at approximately 25 and 35 min on capillary zone electrophoresis. Diode array spectral analysis detected indistinguishable characteristics between these two protein peaks. In addition, complex formation of these components with patients' immunoglobulin was demonstrated by capillary zone electrophoresis. Analysis of components separated by SDS-PAGE on a polyvinylidene difluoride membrane showed that the first 13 residues were identical to the sequence of hevein. Based on the criteria of charge-to-mass ratio and N-terminall amino acid sequence, our results suggest that these components of latex proteins are similar in the primary structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02255930
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Phosphorylation of human interleukin-2 (IL-2) (1989)
    Springer
    Molecular and cellular biochemistry 89 (1989), S. 29-35 
    Details
    ISSN: 1573-4919
    Keywords: interleukin-2 ; protein kinase C ; radioactive labeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Human interleukin-2 (IL-2) is a lymphokine which is capable of activating lymphocytes and supporting the long-term in vitro growth of activated T cell clones. Recombinant human IL-2, expressed in either E. coli or cos cells, was shown to be phosphorylated by protein kinase C. Phosphorylated IL-2 synthesized in E. coli was analyzed by SDS-PAGE, reverse phase HPLC, and tryptic peptide mapping. The phosphorylated tryptic peptide was identified as the N-terminal fragment containing a single phosphorylation site at the serine residue at position 7. There was no difference in biological activity between non-phosphorylated and phosphorylated IL-2, as determined by a T cell growth assay. Although the physiological role of phosphorylation of IL-2 is unclear, IL-2 can be labeled with [γ-32p] ATP and protein kinase C to a high specific radioactivity, and the synthesis of biologically active 32p-labeled IL-2 may be useful for receptor-binding studies of the cells containing low level of phosphoprotein phosphotases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00228277
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Conformational effects of amino acid substitutions at positions 10, 12, and 13 in the P21 protein (1989)
    Springer
    The protein journal 8 (1989), S. 79-86 
    Details
    ISSN: 1573-4943
    Keywords: conformational energy ; amino acid substitution ; P21 protein ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Substitutions of amino acids for Gly 12 or Gly 13 in theras oncogene-encoded P21 proteins have been demonstrated to produce unique structural changes in these proteins that correlate with their ability to produce cell transformation. For example, the P21 proteins with Arg 12 or Val 13 are both known to be actively transforming. Recent site-specific mutagenesis experiments on the transforming Arg 12 protein have found that the substitution of Val for Gly 10 has no effect on transforming activity whereas the substitution of Val for Gly 13 led to a loss of transforming activity. In this study, we examine the structural effects of these substitutions on the amino terminal hydrophobic decapeptide (Leu 6-Gly 15) of P21 using conformational energy analysis. The results show that the transforming proteins with Gly 10 and Arg 12 or Val 10 and Arg 12 can both adopt the putative malignancy-causing conformation, whereas, for the nontransforming protein with Arg 12 and Val 13, this conformation is energetically disallowed. These results further support the theory that due to structural changes the transforming P21 proteins are unable to bind to some regulatory cellular element which may be the recently identified binding protein responsible for the induction of increased GTPase activity in normal P21 compared with transforming mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025080
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  • 4
    Electronic Resource
    Electronic Resource
    Autoregulation of the rho gene of Escherichia coli K-12 (1984)
    Springer
    Molecular genetics and genomics 193 (1984), S. 210-213 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary It has previously been proposed, based on indirect evidence, that the Rho protein may control the expression of the rho gene. Using an in vitro system for the transcription and translation of the rho gene cloned into plasmid pBR322, we tested this hypothesis directly by monitoring the effect in vitro of excess or limiting Rho protein. The addition of purified Rho protein suppresses Rho synthesis in vitro. The addition of antibody to Rho specifically stimulates Rho synthesis in vitro. The stimulation of Rho factor synthesis by antibody to Rho is reversed by Rho protein. Rho factor purified from a strain with a mutationally altered rho gene (rho-115) does not suppress Rho synthesis in vitro. These results provide convincing evidence that the rho gene is subject to autoregulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330669
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