Guanidine-Chloride Stripping Buffer

2020 ◽  
Vol 2020 (3) ◽  
pp. pdb.rec101147
Keyword(s):  
Guanidine Chloride

scholarly journals Expression and Isolation of N-Terminal Truncated Human Recombinant Renalase in Prokaryotic Cells

2021 ◽  
Vol 4 (3) ◽  
pp. e00158
Author(s):  
V.I. Fedchenko ◽  
A.A. Kaloshin ◽  
S.A. Kaloshina ◽  
A.E. Medvedev
Keyword(s):  
Recombinant Protein ◽  
Signal Peptide ◽  
Extracellular Space ◽  
Inclusion Bodies ◽  
High Concentration ◽  
Genetic Construct ◽  
E Coli ◽  
Insoluble Form ◽  
Guanidine Chloride ◽  
Catalytic Functions

Renalase (RNLS) is a flavoproteinin which its N-terminal peptide (residues 1-17) has several important functions. In cells, it participates in the formation of the so-called Rossmanfold (residues 2-35), needed for «accommodation» of the FAD cofactor and for performing the catalytic functions of RNLS as a FAD-dependent oxidoreductase (EC 1.6.3.5). RNLS secretion into the extracellular space is accompanied by cleavage of this peptide. The resultant truncated extracellular RNLS cannot bind FAD and therefore performs various noncatalytic functions. In this work, we have performed expression the genetic construct encoding RNLS lacking its N-terminal signal peptide (tRNLS) in E. coli Rosetta (DE3) cells. The recombinant protein was accumulated in inclusion bodies in an insoluble form, which could be solubilized in the presence of a high concentration of urea or guanidine chloride. In contrast to full-length RNLS, which was effectively solubilized in the presence of 8 M urea, tRNLS was preferentially solubilized in the presence of 6 M guanidine chloride.

High concentrations of guanidine chloride activate lactate dehydrogenase in low water media

1990 ◽  
Vol 172 (2) ◽  
pp. 830-834 ◽  
Author(s):  
Georgina Garza-Ramos ◽  
Alberto Darszon ◽  
M.Tuena de Gómez-Puyou ◽  
A. Gómez-Puyou
Keyword(s):  
Lactate Dehydrogenase ◽  
Water Media ◽  
Guanidine Chloride ◽  
High Concentrations

A short, unsupported Cu(i)⋯Cu(i) interaction, 2.65 Å, in a dinuclear guanidine chloride complex

2010 ◽  
Vol 46 (1) ◽  
pp. 136-138 ◽  
Author(s):  
Gina M. Chiarella ◽  
Doris Y. Melgarejo ◽  
Alex Rozanski ◽  
Pierre Hempte ◽  
Lisa M. Perez ◽  
...  
Keyword(s):  
Chloride Complex ◽  
Guanidine Chloride

scholarly journals Enhancing Colorimetric LAMP Amplification Speed and Sensitivity with Guanidine Chloride

2020 ◽  
Author(s):  
Yinhua Zhang ◽  
Guoping Ren ◽  
Jackson Buss ◽  
Andrew J. Barry ◽  
Gregory C. Patton ◽  
...  
Keyword(s):  
Guanidine Hydrochloride ◽  
Diagnostic Methods ◽  
Molecular Diagnostic ◽  
Simple Method ◽  
Diagnostic Assays ◽  
Dna And Rna ◽  
Target Dna ◽  
Versatile Technique ◽  
Guanidine Chloride ◽  
Primer Sets

AbstractLoop-mediated isothermal amplification (LAMP) is a versatile technique for detection of target DNA and RNA, enabling rapid molecular diagnostic assays with minimal equipment. The global SARS-CoV-2 pandemic has presented an urgent need for new and better diagnostic methods, with colorimetric LAMP utilized in numerous studies for SARS-CoV-2 detection. However, the sensitivity of colorimetric LAMP in early reports has been below that of the standard RT-qPCR tests, and we sought to improve performance. Here we report the use of guanidine hydrochloride and combined primer sets to increase speed and sensitivity in colorimetric LAMP, bringing this simple method up to the standards of sophisticated technique and enabling accurate and high-throughput diagnostics.

Activity of heart and muscle lactate dehydrogenases in all-aqueous systems and in organic solvents with low amounts of water. Effect of guanidine chloride

1992 ◽  
Vol 205 (2) ◽  
pp. 501-508 ◽  
Author(s):  
D. Alejandro FERNANDEZ-VELASCO ◽  
Georgina GARZA-RAMOS ◽  
Leticia RAMIREZ ◽  
Liora SHOSHANI ◽  
Alberto DARSZON ◽  
...  
Keyword(s):  
Organic Solvents ◽  
Aqueous Systems ◽  
Water Effect ◽  
Muscle Lactate ◽  
Guanidine Chloride ◽  
Lactate Dehydrogenases

scholarly journals Interaction between ATP, oleandomycin and the OleB ATP-binding cassette transporter of Streptomyces antibioticus involved in oleandomycin secretion

1997 ◽  
Vol 321 (1) ◽  
pp. 139-144 ◽  
Author(s):  
André BUCHE ◽  
Carmen MÉNDEZ ◽  
José A. SALAS
Keyword(s):  
Fusion Protein ◽  
Nucleotide Binding ◽  
Intrinsic Fluorescence ◽  
Atp Binding ◽  
Hydrophobic Membrane ◽  
Streptomyces Antibioticus ◽  
Binding Domains ◽  
Atp Binding Cassette Transporter ◽  
Guanidine Chloride ◽  
Atp Binding Cassette

The OleB protein of Streptomyces antibioticus, oleandomycin (OM) producer, constitutes an ATP-binding cassette transporter containing two nucleotide-binding domains and is involved in OM resistance and its secretion in this producer strain. We have characterized some properties of the first nucleotide-binding domain of OleB using an overexpressed fusion protein (MBP–OleB´) between a maltose-binding protein (MBP) and the first half of OleB (OleB´). Extrinsic fluorescence of the base-modified fluorescent nucleotide analogue 1,N6-ethenoadenosine 5´-triphosphate (εATP) and 2´(3´)-o-(2,4,6-trinitrophenyl)adenosine-5´-triphosphate was determined in the presence of MBP and the fusion protein MBP–OleB´, and it was found that εATP binds to MBP–OleB´ with a stoichiometry of 0.9. Measurements of the intrinsic fluorescence of the MBP–OleB´ fusion protein indicated that ATP induces a decrease in the accessibility of the MBP–OleB´ tryptophans to acrylamide, an indication of a folding effect. This conclusion was confirmed by the fact that ATP also induces considerable stabilization against guanidine chloride denaturation of MBP–OleB´. Two effects were found to be associated with the presence of Mg2+ ions: (1) an increase in the quenching of MBP–OleB´ intrinsic fluorescence by ATP; and (2) an increase in the accessibility of MBP–OleB´ tryptophans to acrylamide. Significant changes in the intrinsic fluorescence of the fusion protein were also observed in the presence of OM, demostrating the existence of interaction between the transporter and the antibiotic in the absence of any hydrophobic membrane component.

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