Study of the Molecular Forces Involved in the Gelation of Plasma Proteins at Alkaline pH

摘要

ABSTRACTThe effects of vaious reagents on the rheological properties of heat‐induced (90°C) gels formed from plasma protein solutions (pH 9.0) were studied. Both propylene glycol (5–20, w/v) and ethanol (5–20,, w/v), which enhance hydrogen and electrostatic interactions, increased gel compressive strength, whereas mercaptoethanol (25–100 mM) which reduces disulfides, and the sulfhydryl‐blocking agent,p‐hydroxymcrcuribenzoate (25–100 mM), reduced gel strength. High levels of guanidine hydrochloride (>1M) or urea (>2M), which weaken both hydrogen and hydrophobic interactions, decreased gel strength. On the basis of the results, we conclude that hydrophobic interactions and hydrogen and disulfide bonding are involved in the gelation of p