Determination of restriction endonuclease activity in toluene lysates of bacterial cells

1984 ◽  
Vol 97 (2) ◽  
pp. 183-185 ◽  
Author(s):  
N. N. Sokolov ◽  
A. B. Fitsner ◽  
�. B. Khoroshutina ◽  
M. Ya. Kheislere
Keyword(s):  
Restriction Endonuclease ◽  
Bacterial Cells ◽  
Endonuclease Activity

An Electrochemical Assay for Restriction Endonuclease Activity Using Graphene Monolayer

2014 ◽  
Vol 161 (12) ◽  
pp. B261-B264 ◽  
Author(s):  
Kamrul Islam ◽  
Rohit Chand ◽  
Dawoon Han ◽  
Ik-Soo Shin ◽  
Yong-Sang Kim
Keyword(s):  
Restriction Endonuclease ◽  
Graphene Monolayer ◽  
Endonuclease Activity ◽  
Electrochemical Assay

Influence of Resin Monomers on Growth of Oral Streptococci

2004 ◽  
Vol 83 (4) ◽  
pp. 302-306 ◽  
Author(s):  
Y. Takahashi ◽  
S. Imazato ◽  
R.R.B. Russell ◽  
Y. Noiri ◽  
S. Ebisu
Keyword(s):  
Morphological Observation ◽  
Bacterial Suspension ◽  
Bacterial Cells ◽  
Oral Streptococci ◽  
Streptococcus Sobrinus ◽  
Associated Bacteria ◽  
Streptococcus Sanguis ◽  
Colony Forming Units ◽  
Biomass Increase

Ethyleneglycol dimethacrylate monomers have been previously reported to stimulate the growth of certain caries-associated bacteria on the basis of turbidity measurements. To elucidate the detail of this effect, we examined the influence of resin monomers on the growth of Streptococcus sobrinus and Streptococcus sanguis by determination of bacterial numbers (colony-forming units), morphological observation, and chemical analysis. Although the absorbance values in the stationary phase of bacterial suspension were increased in the presence of ethyleneglycol monomers, no significant differences were observed for bacterial numbers throughout the incubation period. Scanning electron microscopy observation revealed the formation of sparse vesicular material surrounding bacterial cells when incubated with ethyleneglycol monomers, and these products were proved to be resin polymers. The results demonstrate that the apparent biomass increase during incubation with ethyleneglycol monomers is due not to promotion of bacterial multiplication, but to the polymerization of resin monomers to form vesicular structures attached to cells.

Ultrasensitive fluorometric determination of iron(iii) and inositol hexaphosphate in cancerous and bacterial cells by using carbon dots with bright yellow fluorescence

The Analyst ◽  
2019 ◽  
Vol 144 (16) ◽  
pp. 5010-5021 ◽  
Author(s):  
Fangchao Cui ◽  
Jiadi Sun ◽  
Xingxing Yang ◽  
Jian Ji ◽  
Fuwei Pi ◽  
...  
Keyword(s):  
Living Cells ◽  
Dual Function ◽  
Bacterial Cells ◽  
Trace Detection ◽  
Ferric Ions ◽  
Fluorometric Determination ◽  
Inositol Hexaphosphate ◽  
Yellow Fluorescence ◽  
Bright Yellow

An ON–OFF–ON dual-function fluorescent nanoprobe is described for the trace detection of ferric ions and inositol hexaphosphate (IP6) in living cells.

Learning the ABCs one at a time: structure and mechanism of ABC transporters

2019 ◽  
Vol 47 (1) ◽  
pp. 23-36 ◽  
Author(s):  
Robert C. Ford ◽  
Konstantinos Beis
Keyword(s):  
Abc Transporters ◽  
Atp Hydrolysis ◽  
Atp Binding ◽  
Bacterial Cells ◽  
The Novel ◽  
Mechanism Model ◽  
Binding Domains ◽  
Atp Binding And Hydrolysis ◽  
Alternating Access

Abstract ATP-binding cassette (ABC) transporters are essential proteins that are found across all kingdoms of life. ABC transporters harness the energy of ATP hydrolysis to drive the import of nutrients inside bacterial cells or the export of toxic compounds or essential lipids across bacteria and eukaryotic membranes. Typically, ABC transporters consist of transmembrane domains (TMDs) and nucleotide-binding domains (NBDs) to bind their substrate and ATP, respectively. The TMDs dictate what ligands can be recognised, whereas the NBDs are the power engine of the ABC transporter, carrying out ATP binding and hydrolysis. It has been proposed that they utilise the alternating access mechanism, inward- to outward-facing conformation, to transport their substrates. Here, we will review the recent progress on the structure determination of eukaryotic and bacterial ABC transporters as well as the novel mechanisms that have also been proposed, that fall out of the alternating access mechanism model.

scholarly journals A Simple Protocol for the Determination of Lysostaphin Enzymatic Activity

Antibiotics ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 917
Author(s):  
Alexander V. Grishin ◽  
Svetlana V. Konstantinova ◽  
Irina V. Vasina ◽  
Nikita V. Shestak ◽  
Anna S. Karyagina ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Catalytic Efficiency ◽  
Bacterial Cells ◽  
Binding Domains ◽  
Simple Protocol ◽  
Specialized Equipment ◽  
Osmotic Lysis ◽  
Cross Bridges ◽  
Bacterial Peptidoglycan

Antibacterial lysins are enzymes that hydrolyze bacterial peptidoglycan, which results in the rapid death of bacterial cells due to osmotic lysis. Lysostaphin is one of the most potent and well-studied lysins active against important nosocomial pathogen Staphylococcus aureus. Similarly to most other lysins, lysostaphin is composed of enzymatic and peptidoglycan-binding domains, and both domains influence its antibacterial activity. It is thus desirable to be able to study the activity of both domains independently. Lysostaphin cleaves pentaglycine cross-bridges within the staphylococcal peptidoglycan. Here, we report the protocol to study the catalytic activity of lysostaphin on the isolated pentaglycine peptide that is based on the chromogenic reaction of peptide amino groups with ninhydrin. Unlike previously reported assays, this protocol does not require in-house chemical synthesis or specialized equipment and can be readily performed in most laboratories. We demonstrate the use of this protocol to study the effect of EDTA treatment on the lysostaphin enzymatic activity. We further used this protocol to determine the catalytic efficiency of lysostaphin on the isolated pentaglycine and compared it to the apparent catalytic efficiency on the whole staphylococcal cells. These results highlight the relative impact of enzymatic and peptidoglycan-binding domains of lysostaphin on its bacteriolytic activity.

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