Comparison of bacteriolytic activity of human interleukin-2 and chicken egg lysozyme on Lactobacillus plantarum and Escherichia coli cells

2015 ◽  
Vol 70 (6) ◽  
pp. 287-291 ◽  
Author(s):  
P. A. Levashov ◽  
D. A. Matolygina ◽  
H. E. Osipova ◽  
S. S. Savin ◽  
G. S. Zaharova ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactobacillus Plantarum ◽  
Interleukin 2 ◽  
Bacteriolytic Activity ◽  
Chicken Egg ◽  
Escherichia Coli Cells

scholarly journals Characterization of human interleukin 2 derived from Escherichia coli

1985 ◽  
Vol 229 (2) ◽  
pp. 429-439 ◽  
Author(s):  
S M Liang ◽  
B Allet ◽  
K Rose ◽  
M Hirschi ◽  
C M Liang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dna Sequence ◽  
Protein A ◽  
Interleukin 2 ◽  
Coding Region ◽  
Disulphide Bridge ◽  
E Coli ◽  
Escherichia Coli Cells

Interleukin 2 isolated from Escherichia coli cells expressing the human interleukin gene has been characterized. The observed properties of the protein have been compared with those properties which can be deduced from the DNA sequence alone and the published properties of natural human interleukin 2. The purified E. coli-derived interleukin 2 is a monomeric protein of Mr 15 000 with a sedimentation velocity of 1.86S. The amino acid composition of the protein and isoelectric point (7.7) are consistent with that part of the translated DNA sequence of the gene corresponding to the mature protein. A single disulphide bridge was identified between Cys-58 and Cys-105. C.d. suggested that interleukin 2 is predominantly alpha-helical in secondary structure. The E. coli-derived protein differed from natural interleukin 2 in the presence of N-terminal methionine and also in the absence of a carbohydrate moiety. Removal of the coding region for the first three amino acids of the natural interleukin 2 protein sequence (Ala-Pro-Thr) by site-specific mutagenesis resulted in a protein with N-terminal serine. The possibility that the specificity of the E. coli ribosomal methionine aminopeptidase may not recognize the sequence NH2-Met-Xaa-Pro is discussed (where Xaa is any amino acid residue).

scholarly journals Bacteriolytic Activity Of Human Interleukin-2, Chicken Egg Lysozyme In The Presence Of Potential Effectors

Acta Naturae ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 82-87 ◽  
Author(s):  
P. A. Levashov ◽  
D. A. Matolygina ◽  
E. D. Ovchinnikova ◽  
D. L. Atroshenko ◽  
S. S. Savin ◽  
...  
Keyword(s):  
Concentration Dependence ◽  
Aromatic Amines ◽  
Interleukin 2 ◽  
Aromatic Amino Acids ◽  
Maximum Activity ◽  
Peptide Antibiotics ◽  
Activity Maximum ◽  
Bacteriolytic Activity ◽  
Chicken Egg ◽  
Micromolar Range

The bacteriolytic activity of interleukin-2 and chicken egg lysozyme in the presence of various substances has been studied. Glycine and lysine do not affect the activity of interleukin-2 but increase that of lysozyme, showing a bell-shape concentration dependence peaking at 1.5 mM glycine and 18 mM lysine. Arginine and glutamate activate both interleukin-2 and lysozyme with a concentration dependence of the saturation type. Aromatic amino acids have almost no effect on the activity of both interleukin-2 and lysozyme. Aromatic amines, tryptamine, and tyramine activate interleukin-2 but inhibit lysozyme. Peptide antibiotics affect interleukin and lysozyme similarly and exhibit maximum activity in the micromolar range of antibiotics. Taurine has no effect on the activity of interleukin-2 and lysozyme. Mildronate showed no influence on lysozyme, but it activated interleukin-2 with the activity maximum at 3 mM. EDTA activates both interleukin-2 and lysozyme at concentrations above 0.15 mM.

DETECTION OF GAMMA RADIATION EFFECT INDUCED BY COBELT-60 ON ESCHERICHIA COLI CELLS

2010 ◽  
Vol 13 (3) ◽  
pp. 129-133
Author(s):  
Ghusoon Ali Abdul Hasan Al-Sudany ◽  
◽  
Wasan Zuheir Majeed ◽  
Hind Jabbar Abdul Rhman Akram Al-Aubeidi ◽  
◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gamma Radiation ◽  
Radiation Effect ◽  
Escherichia Coli Cells

scholarly journals AES and ToF-SIMS combination for single cell chemical imaging of gold nanoparticle-labeled Escherichia coli

2021 ◽  
Author(s):  
Cecile COURREGES ◽  
Mélanie Bonnecaze ◽  
Delphine Flahaut ◽  
Sophie Nolivos ◽  
Regis Grimaud ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gold Nanoparticles ◽  
Single Cell ◽  
Electron Spectroscopy ◽  
Auger Electron ◽  
Chemical Imaging ◽  
Single Cell Level ◽  
Cell Level ◽  
Tof Sims ◽  
Escherichia Coli Cells

A chemical fingerprint of Escherichia coli cells surface labeled by gelatin coated gold nanoparticles was obtained by combining Auger Electron Spectroscopy (AES) for single cell level chemical images, and Time-of-Flight...

Sign in / Sign up

Export Citation Format

Share Document