Results 221 to 230 of about 167,532 (264)
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An automated colorimetric mutarotase assay

Analytical Biochemistry, 1966
Abstract A fully automated mutarotase assay capable of measuring thirty samples per hour or monitoring the effluent from a column is presented. A procedure for partially purifying tissue extracts for the assay is described. Comparisons with a polarimetric assay are given.
J B, Hill, D S, Cowart
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Colorimetric Assay of Tetracycline Antibiotics

Journal of Pharmaceutical Sciences, 1971
A sensitive colorimetric method of analysis for seven compounds of the tetracycline series was developed, based on the formation of a colored complex between the tetracyclines and quadrivalent thorium. The effects of pH and time upon the stability of the complexes were observed.
L G, Chatten, S I, Krause
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Arylsulfatases: Colorimetric and fluorometric assays

1987
Publisher Summary This chapter discusses the colorimetric and fluorometric assays of arylsulfatases. The assay of arylsulfatases is simple in principle, and any of the reaction products may be determined. The general method is simple and requires only that the reaction mixture, after incubation with the enzyme, be made alkaline so that the liberated ...
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A colorimetric assay for γ-glutamyltranspeptidase

Clinica Chimica Acta, 1971
A highly sensitive and simple colorimetric method for the assay of γ-glutamyltranspeptidase is described. As substrate, l-γ-glutamyl-p-nitroanilide has been used, which is dissolved with glycylglycine and MgCl2 in ammediol—HCl buffer. The enzyme splits the substrate in the γ-glutamyl group and p-nitroaniline, the γ-glutamyl group is bound by the ...
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A colorimetric method for assaying citrulline

Analytical Biochemistry, 1969
Abstract A method is available for assaying 0.1 to 1.0 m M citrulline. Urea, carbamyl phosphate, and carbamyl aspartate do not interfere with the citrulline assay.
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A Colorimetric Esterase Assay

1990
Abstract : Using rat serum as a source of esterase activity, we describe a quick and efficient method of taking advantage of the water solubility of the paranitrophenoxide anion. Esterase activity is terminated by adding chloroform and releasing paranitrophenol converted to the 400 nanometers absorbing paranitrophenoxide anion by adding 0.2 molar ...
James P. Chambers, James J. Valdes
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A colorimetric formaldehyde assay

Applied Biochemistry and Biotechnology, 1997
A room-temperature assay of formaldehyde is described. The assay uses few reagents and is colorimetric, read at a wavelength of 649 nm. Tryptophan and tryptamine were noted as interfering with the assay, probably by binding with the formaldehyde. High levels of sugar show smaller effects on final absorbance. Glyceraldehyde also reacts in the assay, but
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A colorimetric fructose assay

Applied Biochemistry and Biotechnology, 1995
A new spectrophotometric method for measuring fructose is presented. The method uses Tryptamine in HCl acid, is carried out at 60°C, and is complete within 60 min. The assay is read at 518 nm and shows very low interference from other sugars. The method can be used for fructose, fructosans, and inulin.
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Colorimetric assay for chitinase

1988
Publisher Summary This chapter describes the colorimetric assay for chitinase, which is applicable to the various types of chitinase present in microorganisms, animals, and plants. The chapter evaluates it with particular reference to plant chitinases, because they may function as a defense against chitin-containing pathogens.
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Colorimetric Assay of Amphotericin B

Journal of Pharmaceutical Sciences, 1963
J C, CHANG   +3 more
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