Treatment of Meningitis With Sulfadiazine and Sulfamerazine

Zeller, William W.; Hirsh, Harold L.; Sweet, Lewis K.; Dowling, Harry F.

doi:10.1001/jama.1948.02890180010003

Cited by 16 publications

(4 citation statements)

References 12 publications

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“…L-Amino-acid oxidase. Measurements of 02 uptake obtained after addition of 002M-L-leucine to solutions of venom in phosphate buffer, pH 7 4, were made (Zeller, 1948).…”

Section: Methodsmentioning

confidence: 99%

Enzyme inhibitions by snake venoms

Braganca

Quastel

1953

Biochemical Journal

117

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Jones gave constant help and encouragement, while Dr T. F. Gallagher was generous in providing pure reference compounds. I am also indebted to many other members of the staff of the Sloan-Kettering Institute for their unfailing courtesy and patience. This work was done during the tenure of an American Government grant under the Fulbright and Smith-Mundt Acts. Additional funds were kindly made available by the Trustees of the Sloan-Kettering Institute.

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“…L-Amino-acid oxidase. Measurements of 02 uptake obtained after addition of 002M-L-leucine to solutions of venom in phosphate buffer, pH 7 4, were made (Zeller, 1948).…”

Section: Methodsmentioning

confidence: 99%

Enzyme inhibitions by snake venoms

Braganca

Quastel

1953

Biochemical Journal

117

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“…form heteromeric associations with collagenic or hydrophobic proteins, which respectively anchor the enzyme in the basal lamina and in the cell membrane. The venom glands of Bungarus fasciatus contain a soluble monomeric form of enzyme [7,8], AChE S , which possesses a distinct hydrophilic C-terminal peptide, without any cysteine [9]. In order to analyse the catalytic mechanism of AChE and the biosynthetic processes that lead to different AChE forms, AChE has been expressed in several systems.…”

Section: Introductionmentioning

confidence: 99%

Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris

Morel

Massoulié

1997

Biochemical Journal

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In the methylotrophic yeast Pichia pastoris, we expressed the rat acetylcholinesterase H and T subunits (AChEH and AChET respectively), as well as truncated subunits from rat (W553stop or AChETDelta, from which most of the T-peptide was removed) and from Bungarus (V536stop, or AChENAT, or AChEDelta, reduced to the catalytic domain). We show that AChEH and AChET subunits are processed into the same molecular forms as in vivo or in transfected mammalian cells, but that lytic processes converting amphiphilic forms into non-amphiphilic derivatives appear to be more active in yeast. The production of glycophosphatidylinositol (GPI)-anchored molecules (dimers, with a small proportion of monomers) demonstrates that P. pastoris can correctly process a mammalian C-terminal GPI-addition signal. Truncated rat and Bungarus AChE molecules, which exclusively generated non-amphiphilic monomers, were released more efficiently and thus produced more AChE activity. In the hope of increasing the production of AChE, we replaced the endogenous signal peptide by yeast prepeptides, with or without a propeptide. We found that the presence of a propeptide, which does not exist in AChE, does not prevent the proper folding of the enzyme, and that it may either increase or decrease the yield of secreted AChE, depending on the signal peptide. Surprisingly, the highest yield was obtained with the endogenous signal peptide. For all combinations, the yield was 2-3 times higher for Bungarus than for rat AChE, probably reflecting differences in the folding efficiency or stability of the polypeptides. The Michaelis constant (Km), the constant of inhibition by excess substrate (Kss) and the catalytic constant (kcat) values of the recombinant AChEs obtained both in P. pastoris and in COS cells, were essentially identical with those of the corresponding natural enzymes, and the Ki values of active-site and peripheral-site inhibitors (edrophonium, decamethonium, propidium) were similar.

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“…Isoleucine, «-aminoro-butyric acid, citrulline, histidine, leucine, methionine, norleucine, norvaline, phenylalanine, tryptophan, and tyrosine are oxidized in the presence of the enzyme that was used, but the method cannot be used for the determination of histidine and tyrosine because the rate of the reaction is decreased in the presence of the D-configurations of these two amino acids. Benzoic, mandelic, saiicyclic, and iodoacetic acids, sulfonamides, aromatic sulfonic acids, aliphatic «-amino-sulfonic acids, and the carbonyl reagents all inhibit in a competitive manner (8).…”

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confidence: 99%

Specific Enzymatic Determination of Some Alpha-Amino Acids by an Automatic Spectrophotometric Reaction Rate Method.

Malmstadt¹,

Hadjiioannou²

1963

Anal. Chem.

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An automatic spectrophotometric reaction rate method is described for the selective enzymatic determination of about 10-7 equivalents of some L-a-amino acids. The method is based on the coupled enzyme reaction in which oxidative deamination of certain L-a-amino acids is specifically catalyzed by L-amino acid oxidase to form hydrogen peroxide, which reacts with o-dianisidine in the presence of horseradish peroxidase to form a colored reaction product which has its absorption maximum at 440 µ. The time required for the reaction to produce a small fixed amount of colored product, and therefore for the absorbance to change by a preselected amount (about 0.06 unit), is measured automatically and related directly to the initial amino acid concentration. Small volumes (about 4 ml.) of nine different L-a-amino acid solutions were determined in the concentration range of 4 to 50 p.p.m. with relative errors

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Treatment of Meningitis With Sulfadiazine and Sulfamerazine

Cited by 16 publications

References 12 publications

Enzyme inhibitions by snake venoms

Enzyme inhibitions by snake venoms

Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris

Specific Enzymatic Determination of Some Alpha-Amino Acids by an Automatic Spectrophotometric Reaction Rate Method.

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