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4554254 Protein assay by silver binding
PATENT ABSTRACTS
152
4551243 ANAEROBIC DIGESTER John H Martin assigned to Energy Cycle lnc To reduce the accumulation of undesirable solid material within an anaerobic digester, new slurry for digesting is injected into the digester at locations extending across the horizontal width at one end. parallel to a zone of floating solids in a concentration of solid material between ten and twelve percent, with a momentum of at least 0.1 pound-foot per second. Liquid is taken out of the digester across a trough extending across the width of the digester. Bubbles are broken above the liquid level of the digester by a sieve or surfactant or combination of the two.
without tbrmation of hydrogen peroxide, such that in the case of conventional enzymatic methods of the quantitative determination of glucose, cholesterol, neutral fats, free fatty acids, phospholipids or uric acid all existing together with bilirubin in biological fluid, the usual interference with such determination, as otherwise caused by bilirubin coexisting m such fluid, can be prevented by adding such a bilirubin oxidase or laccase together with such a specific additive compound to the determinative reaction system.
4554254 PROTEIN ASSAY BY SILVER BINDING Gerald Krystal, Vancouver, B C, Canadd
4551275 DESMETHYLIMIPRAMINE DERIVATIVES AND POLY(AMINO ACID) CONJUGATES Marcel R Pirio. Prithipal Singh assigned to Syntex(USA)lnc Desmethylimipramine funetionalized compounds are provided for conjugation to antigenic compounds, particularly poly(amino acids) and enzymes. The antigenic conjugates are employed for the production of antibodies, which find particular use in immunoassays for the determination of desmethylimipramine. while the enzyme conjugate finds use in an enzyme assay for the determination of desmethylimipramine.
A novel, inexpensive, highty sensitive and quantitative assay for measuring protein in solution based on the capacity of protein to bind silver is described. In this procedure, protein samples are first treated with glutaraldehyde and then exposed to ammoniacal silver. After a specified time. the reaction is terminated by the addition of sodium thiosulfate and the optical density measured at 420 nm. The useful range of the assay for the majority of standard proteins tested lies between 15 and 2000 ng. This represents a 100-fold increase in sensitivity over the Coomassie Brilliant Blue dye binding procedure. There is little or no interference from carbohydrates, non-ionic detergents or ethanol. Pretreatment of protein samples with Bio-Gel P-2 to remove salts, thiol agents, EDTA and SDS, makes this procedure compatible with most commonly used buffers,
4555490 4554249 METHOD FOR THE QUANTITATIVE DETERMINATION OF PHYSIOLOGICAL COMPONENTS IN B I O L O G I C AL FLUIDS Akira Kosaka, Sawao Murao, Kenich Hirano, Noriak Tanaka, Kuniyosh Matsunaga, Seto. Japan assigned to Amano Pharmaceutical Company Limited A novel enzyme of bilirubin oxidase produced by a genus Myrothecium or genus Coprinus origin microorganism and a conventional enzyme of laccase are found, in the presence of a specific additive compound, e.g. a surface active agent, aromatic carboxylic acid. sulfa drug or protease. 1o oxidize both conjugated and unconjugated bilirubin in biological fluid to biliverdin
RAPID VISUALIZATION SYSTEM FOR GEL ELECTROPHORESIS Carl Merril assigned to The United States of America as represented by the Department of Health and Human Services A method using light ( photodevelopment ) to develop a metallic silver image of biopolymers, particularly nucleic acids and proteins separated on polyacrylamide gels, whereby it is possible to visualize protein and nucleic acid patterns within 10 minutes after electrophoretic separation. This photodevelopment method requires only two solutions: a solution to fix the proteins and a solution containing silver ions, which produces an image x~henexposed to light. This type of protein stain has achieved a sensitivity of about 0.5 ng of protein. DNA separatcd on polyacrylamide may also be visualized with this stain.
152
4551243 ANAEROBIC DIGESTER John H Martin assigned to Energy Cycle lnc To reduce the accumulation of undesirable solid material within an anaerobic digester, new slurry for digesting is injected into the digester at locations extending across the horizontal width at one end. parallel to a zone of floating solids in a concentration of solid material between ten and twelve percent, with a momentum of at least 0.1 pound-foot per second. Liquid is taken out of the digester across a trough extending across the width of the digester. Bubbles are broken above the liquid level of the digester by a sieve or surfactant or combination of the two.
without tbrmation of hydrogen peroxide, such that in the case of conventional enzymatic methods of the quantitative determination of glucose, cholesterol, neutral fats, free fatty acids, phospholipids or uric acid all existing together with bilirubin in biological fluid, the usual interference with such determination, as otherwise caused by bilirubin coexisting m such fluid, can be prevented by adding such a bilirubin oxidase or laccase together with such a specific additive compound to the determinative reaction system.
4554254 PROTEIN ASSAY BY SILVER BINDING Gerald Krystal, Vancouver, B C, Canadd
4551275 DESMETHYLIMIPRAMINE DERIVATIVES AND POLY(AMINO ACID) CONJUGATES Marcel R Pirio. Prithipal Singh assigned to Syntex(USA)lnc Desmethylimipramine funetionalized compounds are provided for conjugation to antigenic compounds, particularly poly(amino acids) and enzymes. The antigenic conjugates are employed for the production of antibodies, which find particular use in immunoassays for the determination of desmethylimipramine. while the enzyme conjugate finds use in an enzyme assay for the determination of desmethylimipramine.
A novel, inexpensive, highty sensitive and quantitative assay for measuring protein in solution based on the capacity of protein to bind silver is described. In this procedure, protein samples are first treated with glutaraldehyde and then exposed to ammoniacal silver. After a specified time. the reaction is terminated by the addition of sodium thiosulfate and the optical density measured at 420 nm. The useful range of the assay for the majority of standard proteins tested lies between 15 and 2000 ng. This represents a 100-fold increase in sensitivity over the Coomassie Brilliant Blue dye binding procedure. There is little or no interference from carbohydrates, non-ionic detergents or ethanol. Pretreatment of protein samples with Bio-Gel P-2 to remove salts, thiol agents, EDTA and SDS, makes this procedure compatible with most commonly used buffers,
4555490 4554249 METHOD FOR THE QUANTITATIVE DETERMINATION OF PHYSIOLOGICAL COMPONENTS IN B I O L O G I C AL FLUIDS Akira Kosaka, Sawao Murao, Kenich Hirano, Noriak Tanaka, Kuniyosh Matsunaga, Seto. Japan assigned to Amano Pharmaceutical Company Limited A novel enzyme of bilirubin oxidase produced by a genus Myrothecium or genus Coprinus origin microorganism and a conventional enzyme of laccase are found, in the presence of a specific additive compound, e.g. a surface active agent, aromatic carboxylic acid. sulfa drug or protease. 1o oxidize both conjugated and unconjugated bilirubin in biological fluid to biliverdin
RAPID VISUALIZATION SYSTEM FOR GEL ELECTROPHORESIS Carl Merril assigned to The United States of America as represented by the Department of Health and Human Services A method using light ( photodevelopment ) to develop a metallic silver image of biopolymers, particularly nucleic acids and proteins separated on polyacrylamide gels, whereby it is possible to visualize protein and nucleic acid patterns within 10 minutes after electrophoretic separation. This photodevelopment method requires only two solutions: a solution to fix the proteins and a solution containing silver ions, which produces an image x~henexposed to light. This type of protein stain has achieved a sensitivity of about 0.5 ng of protein. DNA separatcd on polyacrylamide may also be visualized with this stain.