Solubility Improvement of Shellfish Muscle Proteins by Reaction with Glucose and Its Soluble State in Low-Ionic-Strength Medium

2002 ◽  
Vol 50 (15) ◽  
pp. 4327-4332 ◽  
Author(s):  
Shigeru Katayama ◽  
Junji Shima ◽  
Hiroki Saeki
Keyword(s):  
Ionic Strength ◽  
Muscle Proteins ◽  
Solubility Improvement ◽  
Low Ionic Strength ◽  
Strength Medium ◽  
Soluble State

Differential Coating of Human Red Blood Cells with C4 or C3 in a Low Ionic Strength Medium

Vox Sanguinis ◽  
1981 ◽  
Vol 41 (4) ◽  
pp. 249-254 ◽  
Author(s):  
H. E. Heier ◽  
L. Kornstad ◽  
R. Nordhagen
Keyword(s):  
Ionic Strength ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells ◽  
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.

Gastropod predation sites: the role of predator and prey in chemical attraction of the hermit crab Clibanarius vittatus

1990 ◽  
Vol 70 (3) ◽  
pp. 583-596 ◽  
Author(s):  
D. Rittschof ◽  
C.M. Kratt ◽  
A.S. Clare
Keyword(s):  
Salivary Gland ◽  
Ionic Strength ◽  
Salivary Glands ◽  
Hermit Crab ◽  
Sea Water ◽  
Hermit Crabs ◽  
Muscle Proteins ◽  
Clibanarius Vittatus ◽  
Low Ionic Strength

Gastropod shells are essential to most hermit crabs. Shell availability limits hermit crab populations. Shells provide protection and the degree of shell-fit controls crab growth and fecundity. Crabs locate new gastropod shells from a distance under water by molecules released from gastropod flesh during predation events. Here we test the hypothesis that the salivary glands of the predatory gastropod are the source of enzymes that digest muscle proteins and release peptide attractants. We describe the anatomy of both the acinous salivary glands and the tubular accessory salivary glands of Busycon contrarium which are similar to those of B. carica. The salivary gland ducts empty at the mouth, suggesting a role in the primary digestion of food. We show that gastropod muscle proteins, extracted by salt solutions with the ionic strength of sea water and purified by precipitation in low ionic strength can be digested by gastropod salivary gland enzymes to generate peptides attractive to the hermit crab, Clibanarius vittatus, in field assays.

scholarly journals A Mutant of Sindbis Virus Which Is Released Efficiently from Cells Maintained in Low Ionic Strength Medium

Virology ◽  
1995 ◽  
Vol 210 (2) ◽  
pp. 237-243 ◽  
Author(s):  
Mei-Ling Li ◽  
Victor Stollar
Keyword(s):  
Ionic Strength ◽  
Sindbis Virus ◽  
Low Ionic Strength ◽  
Strength Medium

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

Alteration of Cellular Features after Exposure to Low Ionic Strength Medium

2020 ◽  
pp. 163-179
Author(s):  
Ingolf Bernhardt
Keyword(s):  
Ionic Strength ◽  
Low Ionic Strength ◽  
Strength Medium

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 Properties of Vessel Muscle Proteins extracted with Water or Salt Solutions of Low Ionic Strength

Nature ◽  
1961 ◽  
Vol 189 (4760) ◽  
pp. 230-230 ◽  
Author(s):  
L. LASZT
Keyword(s):  
Ionic Strength ◽  
Muscle Proteins ◽  
Salt Solutions ◽  
Low Ionic Strength
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