TY - JOUR
T1 - The effect of salts upon the pH dependence of the activity of papain and succinyl-papain
AU - Sluyterman, L.A.A.E.
AU - Graaf, de, M.J.M.
PY - 1972
Y1 - 1972
N2 - Papain (EC 3.4.4.10) and succinyl-papain exhibit isoelectric points of 9.6 and 4.3, respectively. The acid limb of the pH activity curve in the pH range of 3.5–4.5 of native papain and the basic limb in the pH range of 8–9 of succinyl-papain are shifted by monovalent salts, whereas the basic limb of native papain and the acid limb of succinyl-papain are not shifted by KCl. The Km and not the kcat with benzoylglycine ethyl ester as substrate is affected by salt. The order of the effectiveness of the ions is I- > NO3- > Br- > Cl- and Li+ > K+. These effects can be explained in terms of non-specific binding of cations and anions and electrostatic interactions.
AB - Papain (EC 3.4.4.10) and succinyl-papain exhibit isoelectric points of 9.6 and 4.3, respectively. The acid limb of the pH activity curve in the pH range of 3.5–4.5 of native papain and the basic limb in the pH range of 8–9 of succinyl-papain are shifted by monovalent salts, whereas the basic limb of native papain and the acid limb of succinyl-papain are not shifted by KCl. The Km and not the kcat with benzoylglycine ethyl ester as substrate is affected by salt. The order of the effectiveness of the ions is I- > NO3- > Br- > Cl- and Li+ > K+. These effects can be explained in terms of non-specific binding of cations and anions and electrostatic interactions.
U2 - 10.1016/0005-2744(72)90247-1
DO - 10.1016/0005-2744(72)90247-1
M3 - Article
SN - 0924-1086
VL - 258
SP - 554
EP - 561
JO - Biochimica et Biophysica Acta, Enzymology
JF - Biochimica et Biophysica Acta, Enzymology
IS - 2
ER -