Some Properties of Succinylated Globin

Abstract

Globin was prepared from porcine hemoglobin according to the method of TYBORet al. Succinyation of globin was carried out using succinic anhydride at pH 8.0-9.0 and some properties of the resulting succinylated globin were investigated. (1) Globin was soluble in water below pH 3.0, but not suffciently soluble at around pH 8.0. Succinylated globin was highly soluble above pH 6.0, though it was slightly so1uble at pH 4.0. (2) Fractional precipitation of globin and succinylated globin was carried out using ammonium sulfate. Globin (pH 2.0) and succinylated globin (pH 7.0) precipitated at 0.1- and 0.4-saturation, respectively. (3) The foaming tests of these protein solution were performed with a reciprocal shaker. The foamability of succinylated globin was superior to that of globin. However, succinylated globin was inferior to globin in foam stability. (4) Asuccinylated globin solution adjusted to pH 2.0 formed jelly-like gel by heating in boiling water for 10min, , whereas gel formation of globin solutions adjusted to pH 2.0, 4.5, 7.0, 9.0 and 11.0 was not observed under similar conditions. (5) Thermocoagulation of ovalbumin was considerably inhibited by addition of globin or succinylated g1obin. The inhibitory effect was maximal when globin-ovalbumin and succinylated globin-ovalbumin were heated at pH 4.0 and pH 6.0, respectively.