TY - JOUR
T1 - The Non‐Specific Electrostatic Nature of the Adsorption of Elastase and Other Basic Proteins on Elastin
AU - Gertler, Arieh
PY - 1971/6
Y1 - 1971/6
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0015244369&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1971.tb01425.x
DO - 10.1111/j.1432-1033.1971.tb01425.x
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C2 - 5104188
AN - SCOPUS:0015244369
SN - 0014-2956
VL - 20
SP - 541
EP - 546
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 4
ER -