Effect of Albumin and Methylated Albumin on the Glucose Permeability of Lipid Membranes

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Abstract
The diffusion of glucose from phospholipid membranes has been measured in the presence of serum albumin or methylated serum albumin. At neutral pH, serum albumin enhanced the rate at which glucose diffused from liposomes containing more than a certain amount of lysolecithin. Net charge of the membrane is not important for the reaction, since positively charged membranes containing stearylamine showed almost the same reactivity as negatively charged liposomes containing dicetyl phosphate. Carboxylmethylated albumin showed enhancement of the diffusion rate of glucose from negatively but not from positively charged liposomes. The amount of methylated albumin required to affect liposomes was much smaller than the amount of albumin required to damage liposomes containing lysolecithin. Cholesterol incorporation suppressed the sensitivity of liposomes to both proteins, albumin and methylated albumin. The effect of temperature and fatty acid composition of phospholipids on the sensitivity of liposomes to proteins suggests the importance of the fluidity of the membrane, especially in the case of methylated albumin.