Electrophoretic behavior of normal human serum albumin at pH4.0. II. Interpretation of electrophoretic patterns in terms of a reversible protein interaction.

Electrophoretic Behavior of Normal Human Serum Albumin at pH 4.0

In the preceding paper on the behavior of pooled normal human serum albumin in various buffers at pH 4.0 (1)) it was demonstrated that the electrophoretic pattern of albumin shows a single moving boundary in the presence of the lower fatty acids, excepting formic and acetic acid, and of certain diand tribasic organic acids. This phenomenon is probably a consequence of the interaction between th...

Characteristic Electrophoretic Patterns of serum protein of Several species of snakes of Iran

Effect of binding of ions and other small molecules on protein structure. VII. The role of aliphatic acid binding and of convection in the electrophoresis of serum albumin at low pH.

Bovine serum albumin undergoes two electrophoretically distinguishable types of interaction in acidic media (1). The first (l-6), which is also shown by ovalbumin, bovine y-pseudoglobulin and oxidized ribonuclease, is observed only in media containing acetate buffer (NaAc-HAc) or other carboxylic acid buffers. The various peaks shown by the electrophoretic patterns obtained in these media corre...

Electrophoretic mobility-ionic strength studies of proteins. IV. The effect of lipids on the electrophoretic patterns of human serum albumin at acid pH.

In previous publications from this laboratory, we have investigated the anomalous behavior of human serum albumin (l), various animal albumins (2) and human -y-globulin (3) in the Tiselius electrophoresis apparatus at acid pH. Because of increasing interest in the behavior of proteins in the acid region below their isoelectric point, this phenomenon has been receiving increasing attention from ...

بررسی ترکیبات گلیکوزیله نهایی آلبومین سرم (AGE) در افراد دیابتی به روش ایزوالکتریک فوکوسینگ (IEF) و فلورسانس جهت ارزیابی پیشرفت بیماری دیابت

Background: The non-enzymatic glycosylation (NEG) of proteins in diabetes damages both the structure and function of these proteins. In vivo and in vitro studies have shown that NEG of proteins and advanced glycosylation end-products (AGE) contribute to the pathogenesis of both macrovascular, such as atherosclerosis, and microvascular complications, such as retinopathy and nephropathy, in diabe...