Some physical-chemical properties of succinylated transferrin, conalbumin, and orosomucoid

Abstract

Reduced-alkylated-succinylated transferrin and conalbumin had random coil conformations in a dilute aqueous buffer solution and had molecular weights near those of native proteins, indicating a lack of subunit structure. Iron served to protect transferrin against denaturation induced in the iron-free protein by succinylation. 10 to 11 fewer amino groups were susceptible to succinylation in the iron-saturated protein than in iron-free transferrin, indicating either the participation of these groups in the iron-binding phenomenon or the fact that iron-saturated transferrin assumes a more compact conformation than iron-free transferrin. Reduced-alkylated-succinylated orosomucoid had a molecular weight close to that of the native protein, however, judging from its β-value of 2.20 · 10 6, it failed to assume a random coil shape in dilute aqueous buffers.