Automatic Precision Glass Electrode

Kraus, Kurt A.; Holmberg, R.W.; Borkowski, C. J.

doi:10.1021/ac60038a034

Cited by 12 publications

(5 citation statements)

References 4 publications

(1 reference statement)

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“…This calls for a pH meter of exceptional stability and sensitivity. A system employing a vibrating reed electrometer as a null detector (Kraus et al, 1950;Bates, 1954) fulfills these requirements.…”

Section: Methodsmentioning

confidence: 99%

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Lebowitz¹,

Laskowski²

1962

Biochemistry

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A potentiometric technique for determination of protein-protein association constants is described. The technique consists of measuring the average number of protons (q) released when solutions of protein A and protein B (at the same pH) are mixed and thus allowed to form complex AB. Relations between q and the apparent association constant, Kapp, were developed and employed. The association constants and q values were determined for trypsin-soybean trypsin inhibitor system at 20.0°in 0.5 M KC1, 0.05 M CaCl2 in the pH range 3.75-5.75 (and, by extrapolation of q, up to pH 8.30). The results are in satisfactory agreement with the few scattered data in the literature. An interesting kinetic phenomenon of "overshoot" in the soybean trypsin inhibitortrypsin association was observed in this study. It was tentatively explained on the assumption that the association reaction is faster than mixing, whereas the dissociation reaction is measurably slow.

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Section: Methodsmentioning

confidence: 99%

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Lebowitz¹,

Laskowski²

1962

Biochemistry

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“…Acidities were determined (25.0°) potentiometrically using a glasscalomel electrode assembly with a vibrating reed electrometer. 13 Results and Discussion Granér and Sillén6 showed that for 0.05 M Bi (III) in 3 M perchlorate, hydrolysis begins near 0.5 H+. The hydroxyl number re14 rises with decreasing acidity but near 0.1 M H+ tends to level at n = ca.…”

Section: Hydrolysis Experimentalmentioning

confidence: 95%

Hydrolytic Behavior of Metal Ions. VIII. Ultracentrifugation of Bismuth(III) in Perchlorate Solution^1,2

Holmberg¹,

Kraus²,

Johnson³

1956

J. Am. Chem. Soc.

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“…An automatic recording equipment for pH measurement or titrations, developed by Kraus et al (37), uses the vibrating reed condenser in attaining balance; a high degree of precision and accuracy is attained. A stabilized circuit for use in detecting end points by a tuning tube ("magic eye") has been developed by Kieselbach (32).…”

Section: Apparatusmentioning

confidence: 99%

Potentiometric Titrations

Furman¹

1951

Anal. Chem.

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Automatic Precision Glass Electrode

Cited by 12 publications

References 4 publications

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Hydrolytic Behavior of Metal Ions. VIII. Ultracentrifugation of Bismuth(III) in Perchlorate Solution^1,2

Potentiometric Titrations

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Automatic Precision Glass Electrode

Cited by 12 publications

References 4 publications

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association*

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association*

Hydrolytic Behavior of Metal Ions. VIII. Ultracentrifugation of Bismuth(III) in Perchlorate Solution1,2

Potentiometric Titrations

Contact Info

Product

Resources

About

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association^*

Hydrolytic Behavior of Metal Ions. VIII. Ultracentrifugation of Bismuth(III) in Perchlorate Solution^1,2