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dc.contributor.authorPatrickios, Costas S.en
dc.contributor.authorYamasaki, E. N.en
dc.creatorPatrickios, Costas S.en
dc.creatorYamasaki, E. N.en
dc.description.abstractExperimental isoelectric points and amine acid compositional data for 58 proteins were compiled and organized. The experimental isoelectric points correlated well with the acidic to basic amino acid molar ratio. This agreement proved the usefulness of a recently presented analytical expression correlating explicitly protein isoelectric point to acid-base composition. Regressed acidic and basic dissociation constants were determined to be pKa = 4.9 and pKb = 10.0, in fair agreement with the expected values of pKa = 4.2 and pKb = 11.2. Theoretical isoelectric points determined by a more complete computational procedure were on the average in as good an agreement with the experimental values as those calculated via the theoretical approximation using the regressed dissociation constants. Thus, the analytical approximation is a powerful tool for the convenient and accurate calculation of protein isoelectric point from the amine acid composition. © 1995 Academic press. Inc.en
dc.sourceAnalytical Biochemistryen
dc.titlePolypeptide amino acid composition and isoelectric point: II. Comparison between experiment and theoryen
dc.description.endingpage91 Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied SciencesΤμήμα Χημείας / Department of Chemistry
dc.description.notes<p>Cited By :65</p>en
dc.contributor.orcidPatrickios, Costas S. [0000-0001-8855-0370]

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