Plasma protein fractions show characteristic differences in their polarographic behavior after being subjected to alkaline digestion. Serum albumin (fraction V) in particular is unique in that it produces a catalytic double-wave in divalent cobalt buffer which increases markedly during the first 10 20 minutes of digestion and then decreases gradually during the following hour. During this same ...

Extraction of house-fly heads with neutral phosphate buffer yielded a dark brown solution from which a number of pigments were separated, either wholly or partially, by chromatography on a column of calcium phosphate mixed with celite. One of the pigments was light-sensitive, and had a yellow color, with a spectral absorption maximum at 437 mmicro in phosphate buffer at pH 6.5. Several consecut...

We used human serum protein fractions to evaluate the sensitivity and bias of three turbidimetric methods for determining concentrations of proteins. Each fraction (Cohn Fractions II, III, IV, and V) was assigned a protein concentration value that was determined by the biuret method, which we calibrated with purified monomer of human serum albumin. All three turbidimetric methods (those involvi...

In simultaneous assays of urinary proteins by the Coomassie Brilliant Blue G-250 (CBB) and the sulfosalicylic acid (SSA) methods, we noticed that about 18% of samples showed about twice higher protein values by the former method than by the latter. Some urinary proteins are soluble in SSA and react with CBB. Examinations with sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed that...

Ion-exclusion/cation-exchange chromatography (IEC/CEC) on a weakly acidic cation-exchange resin using on acidic eluent, developed by Tanaka et al. in 1994, has been employed to monitor the quality of environmental water samples such as acid rainwater and river water, to analyze body fluid samples such as saliva, and to evaluate water purification by photocatalytic materials.1–8 One advantage of...