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  • 1
    Electronic Resource
    Electronic Resource
    Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+ affinity column chromatography (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 196 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5–10 mg of biologically fully active protein per liter culture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10568.x
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  • 2
    Electronic Resource
    Electronic Resource
    RNA synthesis on native DNA complexes isolated from Streptomyces griseus and Escherichia coli (1970)
    Springer
    Archives of microbiology 73 (1970), S. 368-378 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. A native DNA fraction was isolated from the young vegetative mycelium of Streptomyces griseus strain No. 52-1 and was compared with a similar fraction of Escherichia coli B. The endogenous RNA polymerase activities of these DNA fractions were examined. 2. Determining the base composition of the 14C labelled RNA synthesized in vitro, it was found that the conversion of 14C UTP into CMP residue of RNA is negligible in the DNA fraction of S. griseus, while it is significant in the DNA fraction of E. coli. By the proof of density gradient centrifugation, the RNA synthesized in vitro was mainly of messenger size in both species. 3. Template activity of the native DNA fractions was investigated in the presence of isolated E. coli RNA polymerase. When measuring the endogenous RNA polymerase and template activities of the DNA complexes at lower and higher ionic strength it was established that DNA complexes of E. coli under both ionic conditions behaved essentially as free DNA strands did, while endogenous and exogenous RNA polymerase activities in DNA complexes of S. griseus are inhibited in medium of lower ionic strength. Our results indicate the presence of some additional compound in the S. griseus aggregate which is absent in E. coli. This compound could function at lower ionic strength while it would be inactivated at higher ionic strength.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00412303
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  • 3
    Electronic Resource
    Electronic Resource
    Protein phosphatase from rat liver nuclei (1980)
    Springer
    Molecular and cellular biochemistry 32 (1980), S. 13-20 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Protein phosphatase, active on non-histone phosphoprotein substrate, was partially purified from rat liver cell nuclei by means of salt extraction, ammoniumsulfate precipitation, DEAE cellulose chromatography, gel filtration and preparative isoelectrofocusing. Rat liver nuclei contain a heterogenous population of different protein phosphatases. All the enzyme fractions eluted from DEAE cellulose are of low molecular weight between 12,000–31,000. The pH 5.5 peak fraction of preparative isoelectrofocusing was characterized in detail. It has a pH optimum of 6.8 using nuclear phosphoprotein substrate. It is inhibited by Na+ at 80mm, and to a lesser extent by K+, activated by Mg2+(5mm) and Mn2+ (1mm). However, the latter is inhibitory at 6mm. The nuclear protein phosphatase is also active on labelled F1 and F2b histones and casein, however, its V is lower on histones and it contains component(s) active specifically on nuclear phosphoprotein substrate but not on casein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00421292
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