The Non‐Specific Electrostatic Nature of the Adsorption of Elastase and Other Basic Proteins on Elastin

Arieh Gertler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

59 Scopus citations

Abstract

The elastolytic activities of porcine and Streptomyces griseus elastase are inhibited by increased salt concentrations while the proteolytic and esterolytic activities are unaffected. This inhibition results from prevention of adsorption of the latter enzymes on insoluble elastin. Elastase and other basic proteins are adsorbed on elastin in low ionic strength, at pH range of 5–10, whereas acidic proteins are not. The adsorption is salt‐dependent, non‐specific and electrostatic in nature. It results from the formation of salt bonds between the carboxyl groups of elastin and the positively charged groups of the basic proteins. Basic poly(amino acids), that inhibit the elastolytic activity but not the proteolytic or esterolytic activity of porcine elastase by preventing its adsorption on elastin, are also themselves adsorbed on elastin similarly to the natural basic proteins. It was concluded that the elastolytic activity of any basic proteinase depends on two basic properties: ability to be adsorbed on elastin in pH range of 7–10, and side‐chain specificity toward the non‐polar amino acids that form the bulk of amino acid of elastin.

Original languageEnglish
Pages (from-to)541-546
Number of pages6
JournalEuropean Journal of Biochemistry
Volume20
Issue number4
DOIs
StatePublished - Jun 1971

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