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1

Methods for isolation, purification and renaturation of recombinant proteins obtained in Escherichia coli bacteria

100%
Szczepanek A., Plucienniczak A.
Biotechnologia
|
1994
|
issue 4
102-125
EN
Escherichia coli is the most useful bacterial species applied to genetic engineering in recombinant proteins production process.The supply of many polipeptides with potential clinical or industrial use is often limited by their low natural availability. Overexpressed polipeptides may either be located in the cytoplasm and periplasm of E.coli or secreted through the cell membrne into the growth medium.Foreign proteins can be expressed in E.coli cells directly or as fusion proteins with prokaryotic sequences. Frequently, the overexpressed proteins acumulate in the bacterial cytoplasm or periplasm in the form of insoluble inclusion bodies.This review considers isolation, purification, solubiliztion and renaturation of recombinant proteins from E.coli, which is still a serious methodological and technical renaturtion.
2

THe methods for diagnosis of HIV infection

100%
Szczepanek A., Plucienniczak A.
Postępy Higieny i Medycyny Doświadczalnej
|
1994
|
vol. 48
|
issue 4
325-344
EN
The article contains a survay of methods for diagnosis of HIV infection based on detection of various viral markers:antibodies against HIV proteins, HIV-neutralizing antibodies, HIV p24 antigen, fragments of HIV genome or whole virus particles.
3

Isolation and purification of Human Immunodeficiency Virus (HIV) antigens from Escherichia coli bacteria containing HIV genes

100%
Szczepanek A., Plucienniczek A.
Biotechnologia
|
1997
|
issue 2
127-144
EN
Fragments of HIV-1 structural proteins: gp120, gp41, p24, p17 were expressed in E. coli as fusion proteins with N-end fragment of b-galactosidase. To extract the virus fragments from fusion proteins with the use of acid hydrolise, acid-labile bonds Asp-Pro were added at the point of junction. An original method of isolation and purification of inclusion bodies from E. coli cells was developed. The virus peptides obtained were homogeneous on SDS PAGE. These peptides showed no reaction with anti-E. coli antibodies on Western blot test. The level of endotoxin was very low. The obtained virus peptides had strong, antigenic specifity good enough to be used to construct a diagnostic test for the detection of anti-HIV antibodies, that could be used in clinical and scientific research.
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