The application of two-dimensional electrophoretic procedures to structural and genetic studies of seed proteins from Poaceae (including the cultivated cereals) and Fagaceae is described. The following related problems have been considered: covalent and non-covalent association of protein subunits in multiple oligomeric structures; chromosomal locations of genes encoding seed proteins; quantita...

Abstract In this paper, a comparative study was conducted on the extraction effects of six agents for collagen-based mural painting binders. These were used to extract residual proteins in non-aged and thermal aged samples. The protein efficiencies different extracting quantitatively determined by bicinchoninic acid (BCA) method, then processed multivariate analysis variance (MANOVA). impact pr...

Using glycerol as a stabilizing agent, a lysosomal factor (termed “convertase”) which converts the multiple forms of tyrosine aminotransferase has been purified about 16,000-fold with a 6% yield from rat liver. The purification method involves differential centrifugation, salt extraction of the mitochondrial-lysosomal fraction, acetone fractionation, acid precipitation, and chromatography on C...

We describe a procedure for the convenient separation of proteins by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of urine from cases of renal disease. A precipitation method that requires no special apparatus was used to concentrate the urinary proteins; for electrophoretic separation we used a commercially supplied polyacrylamide/cellulose gel slab. This method seems to be valuab...

The acidic chromatin proteins extracted from normal and neoplastic mammary cells of C3H mice and Fischer rats have been compared by polyacrylamide gel electrophoresis, amino acid analysis, and radioactivity labeling patterns of synthesis in vitro. Following purification of chromatin from purified nuclei and extraction of histones in 2 M sodium chloride, the acidic proteins associated with DNA w...

Alkaline phosphatase from human liver was purified to homogeneity. The purification procedure included solubilization with butanol, fractionation with acetone, and chromatography on concanavalin A-Sepharose, DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex. Purity was established by standard and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The isoelectric point of the protein was...

ATP citrate lyase was purified by two different procedures from the livers of rats first starved and then fed with a fat-deficient and high carbohydrate-glycerol diet. These enzyme preparations were judged homogeneous by sedimentation equilibrium and polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was around 4.4 X 10(5) as determined by sedimentation equilibrium. O...

A hemolysin produced by a strain of Aeromonas hydrophila isolated from a patient with diarrhea was purified by acid precipitation and quarternary aminoethyl-Sephadex chromatography. The molecular weight of the hemolysin was estimated at 50,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and at 48,000 by Sephadex G-100 gel filtration. In polyacrylamide gel electrophoresis at pH ...

ATP citrate lyase was purified by two different procedures from the livers of’ rats first starved and then fed with a fat-deficient and high carbohydrate-glycerol diet. These enzyme preparations were judged homogeneous by sedimentation equilibrium and polyacrylamide gel electrophoresis. The molecular weight of the native enzyme was around 4.4 x 105 as determined hy sedimentation equilibrium. On...