PubMed HealthSearch

PubMed · 2024938

Protein interference with ion-selective electrode measurement depends on reference electrode composition and design.

Abstract

There is controversy about whether protein interferes with ion measurements using ion-selective electrodes. We have investigated the effects of changes in the salt-bridge composition of five commercially available analysers with open, membrane-restricted or porous frit-restricted reference electrode junctions on measurements of an albumin solution prepared by gel filtration. When the manufacturers' salt bridges were used, instruments with open or membrane-restricted junctions showed apparent increases in the activity of ionized calcium, sodium and potassium in the presence of protein. When the hypertonic bridge solutions were replaced with 150 mmol/L potassium chloride this increase disappeared. The instrument with a porous frit-restricted junction showed no protein effect, but its response to changes in sample sodium chloride concentration in protein-free solution suggested that its junction was functionally equivalent to that formed with an isotonic sodium chloride bridge. Our results emphasize that liquid junction design and composition affect ion measurements in protein-containing solutions and suggest that the use of hypertonic bridge solutions for biological samples needs to be re-examined.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

R B Payne, B M Buckley, K M Rawson. 1991. Protein interference with ion-selective electrode measurement depends on reference electrode composition and design.. https://doi.org/10.1177/000456329102800111

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

New uses for calcium chloride solution as a mounting medium.

Fresh cross sections of stems (Psilotum nudum, Coleus blumei, and Pelargonium peltatum) and roots (Setcreasea purpurea) 120 microns thick were fixed in FPA50 (formalin: propionic acid: 50% ethanol, 5:5:90, v/v) for 24 hr and stored in 70% ethanol. The sections were transferred to water and then to 1% phloroglucin in 20% calcium chloride solution plus either hydrochloric, nitric, or lactic acid in the following ratios of phloroglucin-CaCl2 solution:acid: 25:4, 20:2, or 15:5. The sections were mounted on slides either in one of the three mixtures or in fresh 20% calcium chloride solution. A rapid reaction of the acid-phloroglucin with lignin produced a deep red color in tracheary elements and an orange-red color in sclerenchyma. Fixed and stored leaf pieces from Nymphaea odorata were autoclaved in lactic acid, washed in two changes of 95% ethanol, transferred to water, and treated with the three acid-phloroglucin-calcium chloride mixtures. The abundant astrosclereids stained an orange-red color similar to that of sclerenchyma in the sections. In addition, a new method is reported for specifically staining lignified tissues. When sections or leaf pieces are stained in aqueous 0.05% toluidine blue O, then placed in 20% calcium chloride solution, all tissues destain except those with lignified or partially lignified cell walls. Thus, toluidine blue O applied as described becomes a reliable specific test for lignin comparable to the acid-phloroglucin test.

Calcium Chloride

Complexoproductive and antiheparin properties of low density lipoproteins (LDL). I. Interaction of isolated low density lipoproteins with heparin of different molecular weight.

Low density lipoproteins/LDL/ form unsoluble complexes with heparin of different molecular weight in the presence of CaCl2. Quantity of the complexes depends on molecular weight of heparin, concentration of reagents and pH of the reacting medium. The biggest quantity of complexes result from LDL-heparin of the molecular weight 16000, the quantity is smaller with heparin of the molecular weight 5100 and the quantity is smallest with heparin of the molecular weight 3700. Components of LDL--heparin complexes are bound by means of ion and hydrogen bonds.

Calcium Chloride

Complexoproductive and antiheparin properties of low density lipoproteins (LDL). II. Interaction of serum low density lipoproteins (LDL) with heparin of different molecular weight.

Quantity of unsoluble LDL complexes with heparin of different molecular weight in hypo-, normo-, and hyperlipemic blood serum in the presence of CaCl2 was estimated. At the same weight concentration the biggest quantity of LDL complexes are formed with heparin with heparin of the molecular weight 16000, the quantity is smaller with heparin of the molecular weight 5100, and it is the smallest with heparin of molecular weight 3700.

Calcium Chloride