1. Sodium error encountered in using a pH meter causes a/an increase in the pH reading of a solution than the actual pH reading. 2. The pH of amino acid is adjusted to 1.5 prior to titration to make sure that the amino acid has a net positive charge. 3. Protein is most soluble in a solution with pH equal to its isoelectric point (IpH).

Curren'S Math For Meds: Dosages & Sol
11th Edition
ISBN:9781305143531
Author:CURREN
Publisher:CURREN
Chapter9: Parenteral Medication Labels And Dosage Calculation
Section: Chapter Questions
Problem 6.7P
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1. Sodium error encountered in using a pH meter causes a/an increase in the pH reading of a solution
than the actual pH reading.
2. The pH of amino acid is adjusted to 1.5 prior to titration to make sure that the amino acid has a net
positive charge.
3. Protein is most soluble in a solution with pH equal to its isoelectric point (IpH).
4. Relatively hydrophilic proteins will require lower amounts of (NH«):SO, to precipitate.
5. Coomassie Brilliant Blue G-250, a dye used in the Bradford assay, has a maximum absorbance at 465
nm when bound with protein.
6. The graph of the amount of precipitate vs pH results in a vertical parabola with a minima near the
sample's isoelectric pH.
Transcribed Image Text:1. Sodium error encountered in using a pH meter causes a/an increase in the pH reading of a solution than the actual pH reading. 2. The pH of amino acid is adjusted to 1.5 prior to titration to make sure that the amino acid has a net positive charge. 3. Protein is most soluble in a solution with pH equal to its isoelectric point (IpH). 4. Relatively hydrophilic proteins will require lower amounts of (NH«):SO, to precipitate. 5. Coomassie Brilliant Blue G-250, a dye used in the Bradford assay, has a maximum absorbance at 465 nm when bound with protein. 6. The graph of the amount of precipitate vs pH results in a vertical parabola with a minima near the sample's isoelectric pH.
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