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260 results on '"Becker MA"'

251. Gout with purine overproduction due to increased phosphoribosylpyrophosphate synthetase activity.

Author

Becker MA, Meyer LJ, and Seegmiller JE

Subjects
Adolescent, Adult, Carbon Isotopes, Child, Erythrocytes metabolism, Female, Fibroblasts, Glycine metabolism, Gout genetics, Guanine, Humans, Hypoxanthines, Lithium metabolism, Male, Middle Aged, Nitrogen metabolism, Pentosyltransferases, Purine-Pyrimidine Metabolism, Inborn Errors enzymology, Purines metabolism, Radioisotopes metabolism, Uric Acid blood, Uric Acid urine, Gout enzymology, Phosphotransferases metabolism, Purines biosynthesis
Published
1973
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252. Epidermolysis bullosa dystrophica.

Author

Scott CI Jr, Becker MA, Houston FM, and Hambrick GW Jr

Subjects
Adolescent, Adrenocorticotropic Hormone therapeutic use, Adult, Anemia etiology, Cicatrix etiology, Contracture etiology, Cortisone therapeutic use, Dental Caries complications, Humans, Male, Osteoporosis complications, Pyridines therapeutic use, Skin pathology, Syndactyly complications, Epidermolysis Bullosa complications, Epidermolysis Bullosa drug therapy, Epidermolysis Bullosa pathology
Published
1971

253. Purine nucleotide synthesis in lymphoblasts cultured from normal subjects and a patient with Lesch-Nyhan syndrome.

Author

Wood AW, Becker MA, and Seegmiller JE

Subjects
Carbon Isotopes, Cell Line, Chromatography, Thin Layer, Diploidy, Humans, Hypoxanthines, Kinetics, Lesch-Nyhan Syndrome metabolism, Pentosephosphates, Phosphoric Acids, Phosphotransferases metabolism, Purine Nucleotides biosynthesis, Purine Nucleotides blood, Lesch-Nyhan Syndrome blood, Lymphocytes metabolism, Nucleotides blood
Published
1973
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254. Increased PP-ribose-P synthetase activity: a genetic abnormality leading to excessive purine production and gout.

Author

Becker MA, Meyer LJ, Kostel PJ, and Seegmiller JE

Subjects
Adenine, Carbon Radioisotopes, Cellulose, Creatinine urine, Electrophoresis, Enzyme Activation, Erythrocytes drug effects, Erythrocytes enzymology, Female, Fibroblasts enzymology, Glycine metabolism, Gout genetics, Guanine Nucleotides, Humans, Hypoxanthines, Male, Pedigree, Pentosephosphates, Pentosyltransferases blood, Phosphates pharmacology, Phosphoric Acids, Uric Acid blood, Uric Acid urine, Gout enzymology, Phosphotransferases blood, Purines metabolism
Published
1973
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255. Effects of nicotinic acid on human fibroblast purine biosynthesis.

Author

Boyle JA, Raivio KO, Becker MA, and Seegmiller JE

Subjects
Adenine, Azaserine pharmacology, Carbon Isotopes, Chromatography, Thin Layer, Diphosphates metabolism, Fibroblasts drug effects, Formates biosynthesis, Formates metabolism, Glycine biosynthesis, Humans, Lesch-Nyhan Syndrome metabolism, Pentosephosphates metabolism, Pentosyltransferases, Ribonucleotides biosynthesis, Ribose metabolism, Skin cytology, Skin drug effects, Skin metabolism, Fibroblasts metabolism, Nicotinic Acids pharmacology, Purines biosynthesis
Published
1972
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256. Pleiotrophy in a cysteine-requiring mutant of Samonella typhimurium resulting from altered protein-protein interaction.

Author

Becker MA and Tomkins GM

Subjects
Animals, Antigens, Chemical Precipitation, Chromatography, DEAE-Cellulose, Chromatography, Gel, Genes, Genetics, Microbial, Hot Temperature, Immune Sera, Immunodiffusion, Methods, Mutation, Phenotype, Precipitin Tests, Rabbits, Serine, Spectrophotometry, Acyltransferases isolation & purification, Cysteine, Lyases isolation & purification, Salmonella typhimurium enzymology
Published
1969

259. Purine overproduction in man associated with increased phosphoribosylpyrophosphate synthetase activity.

Author

Becker MA, Meyer LJ, Wood AW, and Seegmiller JE

Subjects
Adenosine Triphosphate, Carbon Isotopes, Erythrocytes enzymology, Female, Fibroblasts metabolism, Glycine metabolism, Gout blood, Gout genetics, Gout metabolism, Gout urine, Humans, Male, Pentosephosphates, Phosphoric Acids, Uric Acid blood, Uric Acid urine, Gout enzymology, Phosphotransferases metabolism, Purines biosynthesis
Abstract

In hemolyzates from red cells of two brothers with purine overproduction and gout, activity of phosphoribosylpyrophosphate synthetase is more than twofold greater than that measured in normal or other gouty individuals. The increased enzyme activity, which is also demonstrable in fibroblasts of the one patient tested, is associated with increased production of 5-phosphoribosyl-1-pyrophosphate by intact cells, an indication that the enzyme abnormality is the basis for the purine overproduction. This genetic abnormality is an example of an increased enzyme activity producing a disease state.

Published
1973
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260. Human phosphoribosylpyrophosphate synthetase: increased enzyme specific activity in a family with gout and excessive purine synthesis.

Author

Becker MA, Kostel PJ, Meyer LJ, and Seegmiller JE

Subjects
Animals, Electrophoresis, Fibroblasts enzymology, Gout genetics, Humans, Immunoassay, Immunodiffusion, Mutation, Phosphotransferases blood, Purine-Pyrimidine Metabolism, Inborn Errors genetics, Rabbits immunology, Gout enzymology, Phosphotransferases analysis, Purine-Pyrimidine Metabolism, Inborn Errors enzymology
Abstract

Among affected members of a family (B. family) with excessive purine production and gout, activity of phosphoribosylpyrophosphate synthetase (EC 2.7.6.1) is 2.5- to 3.0-fold higher than among normal people. The molecular basis for this increased enzyme activity was studied. Antibody to purified human phosphoribosylpyrophosphate synthetase of erythrocytes was obtained from immunized rabbits. Studies with the IgG fraction of this antiserum show the presence of normal quantities of immunoreactive enzyme, but 2.5- to 3.0-fold higher activity per molecule in affected members of the B. family. In addition, by use of a stain for phosphoribosylpyrophosphate synthetase activity, a difference in electrophoretic mobility was demonstrated on cellulose acetate gel between the partially purified enzyme from normal people and an affected member of the B. family. These studies suggest that the enzyme aberration responsible for purine overproduction and gout in the B. family results from a structurally altered enzyme with increased activity per molecule.

Published
1973
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