Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Efficient Expression of the Paramecium Calmodulin Gene in Escherichia coli after Four TAA-to-CAA Changes through a Series of Polymerase Chain Reactions (1991)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 38 (1991), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We have expressed the Paramecium calmodulin gene in Escherichia coli by changing the four TAA codons in this gene to CAAs. This was carried out by three polymerase chain reactions (PCRs) and then cloning the product into the expression vector pKK223-3 immediately downstream of its trp-lac hybrid promoter. JM109 strain of E. coli, transformed with the recombinant plasmid harboring the altered Paramecium calmodulin gene, produces a protein judged to be calmodulin. It is recognized by a monoclonal antibody to Paramecium calmodulin; it migrates with the native protein at nearly the same rate in electrophoreses; and it shows a Ca2+-dependent shift in electrophoretic pattern. The production of calmodulin is about 170 times as efficient with E. coli as with Paramecium in terms of unit volume of packed cells, and is about 400 times as efficient in unit volume of liquid culture. This method appears useful in site-directed mutageneses and in the heterologous productions of other ciliate proteins. A critique of this method is provided. A calmodulin half-molecule, a by-product of this project, is described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1991.tb04814.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Oral Administration of Avian Tumor Necrosis Factor Antibodies Effectively Treats Experimental Colitis in Rats (2000)
    Springer
    Digestive diseases and sciences 45 (2000), S. 2298-2305 
    Details
    ISSN: 1573-2568
    Keywords: Crohn's disease ; anti-tumor necrosis factor antibody ; oral antibody therapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Tumor necrosis factor (TNF) is implicated in the pathogenesis of inflammatory bowel disease. Clinical trials indicate that intravenous infusion of anti-TNF antibody is an effective therapy for Crohn's disease. An oral anti-TNF therapy may be a preferred approach, reducing systemic side effects and eliminating the inconvenience and expense of administering infusions. We tested oral avian anti-TNF antibodies in the acute and chronic phases of a rodent colitis model. Efficacy was compared to sulfasalazine and dexamethsone. Rats with chemically induced colitis were treated orally with anti-TNF antibody, placebo, or comparator. Efficacy was assessed by change in colonic weight, morphology, histology, and tissue myeloperoxidase activity. Oral anti-TNF antibody, in both the acute and chronic phases of the model, significantly decreased all inflammatory end points and proved to be more effective than sulfasalazine and dexamethasone. Oral delivery of avian anti-TNF antibodies is an effective treatment of experimental colitis and may provide advantages to current parenteral anti-TNF antibodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005554900286
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Primary mutations in calmodulin prevent activation of the Ca+ +-dependent Na+ channel in Paramecium (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 12 (1992), S. 365-371 
    Details
    ISSN: 0887-3585
    Keywords: Amino acid sequence/methylated lysines/protein conformation/Ca+ +-dependent K+ channel/cam behavioral mutants ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Paramecium tetraurelia behavioral mutant cam12 displays a “fast-2” behavioral phenotype: it fails to respond to Na+ stimuli. Electrophysiologically, it lacks a Ca+ +-dependent Na+ current. Genetics and DNA sequencing showed the primary defect of cam12 to be in the calmodulin gene (Kink et al., 1990). To correlate calmodulin structure and function in Paramecium, we elucidated the primary structure of cam12 calmodulin. Peptide sequencing confirmed the two point mutations predicted by the DNA sequence: a glycine-to-glutamate substitution at position 40 and an aspartate-to-asparagine substitution at position 50. Our results further showed that lysine 13 and lysine 115 were methylated normally in cam12. It is likely that the electrophysiological abnormalities of cam12 are a direct reflection of the amino-acid substitutions, as opposed to improper posttranslational modification.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340120408
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...