Insights into the structural characteristic of rabbit glycated myofibrillar protein with high solubility in low ionic strength medium

LWT ◽  
2021 ◽  
Vol 137 ◽  
pp. 110387
Author(s):  
Shaobo Li ◽  
Zhifei He ◽  
Cheng Qu ◽  
Sijie Yu ◽  
Minhan Li ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Structural Characteristic ◽  
Myofibrillar Protein ◽  
High Solubility ◽  
Low Ionic Strength ◽  
Strength Medium

Increased Sensitivity of Tests for the Detection of Blood Group Antigens in Stains Using a Low Ionic Strength Medium

1978 ◽  
Vol 18 (1) ◽  
pp. 16-23 ◽  
Author(s):  
M. J. McDowall ◽  
P. J. Lincoln ◽  
B. E. Dodd
Keyword(s):  
Ionic Strength ◽  
Blood Group ◽  
Red Cells ◽  
Blood Group Antigens ◽  
Additional Advantage ◽  
Suspension Medium ◽  
Increased Sensitivity ◽  
Low Ionic Strength ◽  
Strength Medium

The incorporation of a low ionic strength solution (LISS) in the micro-elution technique used for the detection of blood group antigens in stains markedly improves the test's sensitivity. This is because LISS increases the amount of antibody taken up by the antigen in the stain which results in a greater yield of antibody recovered from the slain by elution. LISS also enhances the activity of the eluted antibody if it is introduced as a suspension medium for the red cells used to detect the antibody. The introduction of suitably diluted AB serum as diluent when testing the eluates is an additional advantage. The improvement in the sensitivity of the micro-elution technique is great enough in some instances to allow the detection of an antigen in a stain which is undetectable in the absence of LISS. Moreover some doubtful positive reactions are enhanced sufficiently for the presence of an antigen to be definitely established.

Actomyosin-like protein of arterial wall

1963 ◽  
Vol 205 (6) ◽  
pp. 1247-1252 ◽  
Author(s):  
Ronald S. Filo ◽  
J. Caspar Ruegg ◽  
David F. Bohr
Keyword(s):  
Ionic Strength ◽  
Atpase Activity ◽  
Arterial Wall ◽  
Structural Protein ◽  
High Solubility ◽  
Viscosity Change ◽  
Relaxing Factor ◽  
Contractile System ◽  
Crude Preparation ◽  
Low Ionic Strength

A structural protein is extractable from hog carotids in solutions of low ionic strength (0.05 m KCl + 0.02 m histidine buffer). The following procedures cause precipitation of this protein: 1) standing 12 hr at 2–4 C, 2) dialysis against 0.05 m KCl, or 3) addition of 10 mm CaCl2. The crude preparation obtained by any of these precipitation procedures fails to show superprecipitation on the addition of ATP, but when dissolved in 0.6 m KCl it does demonstrate a viscosity change on the addition of ATP and is capable of ATPase activity. If this crude preparation is purified by repeated calcium precipitation and dialysis against 0.05 m KCl, it then shows the following characteristics typical of actomyosin: 1) superprecipitation, 2) reversible viscosity change on addition of ATP, and 3) ATPase activity characteristically influenced by calcium, or magnesium, or ionic strength. We conclude that this structural protein from hog carotid is an actomyosin-like protein involved in a standard contractile system, and its initial high solubility at low ionic strength may be due either to a reduction in bound calcium or to the presence of an unusually effective solubilizing factor which, like relaxing factor, can be inhibited by calcium.

scholarly journals Contributions of MexAB-OprM and an EmrE Homolog to Intrinsic Resistance of Pseudomonas aeruginosa to Aminoglycosides and Dyes

2003 ◽  
Vol 47 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Xian-Zhi Li ◽  
Keith Poole ◽  
Hiroshi Nikaido
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Ionic Strength ◽  
Ethidium Bromide ◽  
Luria Broth ◽  
Drug Susceptibility ◽  
Intrinsic Resistance ◽  
Aminoglycoside Resistance ◽  
Active Efflux ◽  
Low Ionic Strength ◽  
Strength Medium

ABSTRACT Of the six putative small multidrug resistance (SMR) family proteins of Pseudomonas aeruginosa, a protein encoded by the PA4990 gene (emrE Pae) shows the highest identity to the well-characterized EmrE efflux transporter of Escherichia coli. Reverse transcription-PCR confirmed the expression of emrE Pae in the wild-type strain of P. aeruginosa. Using isogenic emrE Pae, mexAB-oprM, and/or mexB deletion mutants, the contributions of the EmrE protein and the MexAB-OprM efflux system to drug resistance in P. aeruginosa were assessed by a drug susceptibility test carried out in a low-ionic-strength medium, Difco nutrient broth. We found that EmrEPae contributed to intrinsic resistance not only to ethidium bromide and acriflavine but also to aminoglycosides. In this low-ionic-strength medium, MexAB-OprM was also shown to contribute to aminoglycoside resistance, presumably via active efflux. Aminoglycoside resistance caused by these two pumps could not be demonstrated in high-ionic-strength media, such as Luria broth or Mueller-Hinton broth. The EmrE-dependent efflux of ethidium bromide was confirmed by a continuous fluorescence assay.

scholarly journals Effect of inorganic polyphosphate on thermal denaturation of carp myofibrillar protein at low ionic strength.

1985 ◽  
Vol 51 (4) ◽  
pp. 667-675 ◽  
Author(s):  
Hiroshi YAGI ◽  
Masahiro SAKAMOTO ◽  
Atsushi WAKAMEDA ◽  
Ken-ichi ARAI
Keyword(s):  
Ionic Strength ◽  
Thermal Denaturation ◽  
Myofibrillar Protein ◽  
Inorganic Polyphosphate ◽  
Low Ionic Strength
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