scholarly journals Potentiometric Investigation of the Dynamics of Bacteriophage - Induced Potassium Ion Efflux in Escherichia coli

2016 ◽  
Vol 01 (01) ◽  
Author(s):  
Galgalkar S
Keyword(s):  
Escherichia Coli ◽  
Potassium Ion ◽  
Ion Efflux

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion

Biochemistry ◽  
1993 ◽  
Vol 32 (33) ◽  
pp. 8560-8567 ◽  
Author(s):  
Matthew J. Todd ◽  
Paul V. Viitanen ◽  
George H. Lorimer
Keyword(s):  
Escherichia Coli ◽  
Potassium Ion ◽  
Hydrolysis Of

scholarly journals Potassium ion efflux induced by cationic compounds in yeast

1999 ◽  
Vol 1418 (1) ◽  
pp. 147-157 ◽  
Author(s):  
Emanuel Enrı́quez-Freire ◽  
Ruth López ◽  
Antonio Peña
Keyword(s):  
Potassium Ion ◽  
Ion Efflux ◽  
Cationic Compounds

scholarly journals Structural and Functional Differences in Two Cyclic Bacteriocins with the Same Sequences Produced by Lactobacilli

2004 ◽  
Vol 70 (5) ◽  
pp. 2906-2911 ◽  
Author(s):  
Yasushi Kawai ◽  
Yasuyuki Ishii ◽  
Kensuke Arakawa ◽  
Koichiro Uemura ◽  
Boku Saitoh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Potassium Ion ◽  
Amino Acid Sequences ◽  
Human Infant ◽  
Composition Analysis ◽  
Molecular Weights ◽  
Functional Differences ◽  
Ion Efflux ◽  
Primary Amino ◽  
Amino Acid Contents

ABSTRACT Lactobacillus gasseri LA39 and L. reuteri LA6 isolated from feces of the same human infant were found to produce similar cyclic bacteriocins (named gassericin A and reutericin 6, respectively) that cannot be distinguished by molecular weights or primary amino acid sequences. However, reutericin 6 has a narrower spectrum than gassericin A. In this study, gassericin A inhibited the growth of L. reuteri LA6, but reutericin 6 did not inhibit the growth of L. gasseri LA39. Both bacteriocins caused potassium ion efflux from indicator cells and liposomes, but the amounts of efflux and patterns of action were different. Although circular dichroism spectra of purified bacteriocins revealed that both antibacterial peptides are composed mainly of α-helices, the spectra of the bacteriocins did not coincide. The results of d- and l-amino acid composition analysis showed that two residues and one residue of d-Ala were detected among 18 Ala residues of gassericin A and reutericin 6, respectively. These findings suggest that the different d-alanine contents of the bacteriocins may cause the differences in modes of action, amounts of potassium ion efflux, and secondary structures. This is the first report that characteristics of native bacteriocins produced by wild lactobacillus strains having the same structural genes are influenced by a difference in d-amino acid contents in the molecules.

New Enzymatic Method with Tryptophanase for Determining Potassium in Serum

1992 ◽  
Vol 38 (1) ◽  
pp. 44-47 ◽  
Author(s):  
Shigeki Kimura ◽  
Seishi Asari ◽  
Sadao Hayashi ◽  
Yoshihisa Yamaguchi ◽  
Ryo Fushimi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Reaction ◽  
Potassium Ion ◽  
Ammonium Ion ◽  
Potassium Ions ◽  
Enzymatic Method ◽  
Ammonium Ions ◽  
E Coli ◽  
Ion Concentrations ◽  
Standard Curve

Abstract We established a simple and rapid enzymatic method for measuring potassium ion in serum by using tryptophanase (EC 4.1.99.1) purified from Escherichia coli K12 strain (E. coli K12 IFO 3301). The presence of pyridoxal 5-phosphate promotes this enzymatic reaction, and potassium and (or) ammonium ions further accelerate it, with ammonium and potassium ions providing equivalent acceleration. We eliminated endogenous ammonium ion by using glutamate dehydrogenase (GLDH; EC 1.4.1.4), then produced ammonium ion in the presence of tryptophanase, tryptophan, and pyridoxal 5-phosphate. The concentration of formed ammonium ion, which was proportional to that of potassium ion in sample, was determined by adding GLDH to produce NADP+ in the presence of 2-oxoglutarate and NADPH; we then read the change of absorbance at 340 nm. The standard curve was linear for potassium ion concentrations up to 7.00 mmol/L. The within-assay variation (CV) was 0.89% at 5.51 mmol/L and 1.32% at 3.37 mmol/L. The day-to-day CVs were 0.99% at 6.85 mmol/L and 1.71% at 3.52 mmol/L. Analytical recoveries ranged from 98.7% to 108.9%. The correlation coefficient between values obtained with this enzymatic assay (y) and by flame photometry (x) was 0.995: y = 0.984x + 0.091 mmol/L (Sy.x = 0.105, n = 100). The presence of hemoglobin, bilirubin, or other cations little affects this system.

Quantitative Analysis of Potassium Ion Pool in Escherichia coli K-121

1979 ◽  
Vol 85 (1) ◽  
pp. 303-310 ◽  
Author(s):  
Hiroto NAKAJIMA ◽  
Ichiro YAMATO ◽  
Yasuhiro ANRAKU
Keyword(s):  
Escherichia Coli ◽  
Quantitative Analysis ◽  
Potassium Ion
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