Results 251 to 260 of about 282,094 (307)
Some of the next articles are maybe not open access.
Colorimetric Assay of Epinephrine
Journal of Pharmaceutical Sciences, 1974A new colorimetric assay method for epinephrine, based on the reaction with thiosemicarbazide in alkaline medium, is presented. Beer's law is followed in the range of 25–300 μg. Data on precision, accuracy, and specificity are included. A special calculation is adopted in the presence of norepinephrine.
R B, Salama, S K, Khalil
openaire +2 more sources
Colorimetric Assay of Disulfiram
Journal of Pharmaceutical Sciences, 1973A quantitative assay for disulfiram was developed based on color formation during the interaction of disulfiram, ethanol, and cyanide. A linear curve is obtained over a wide range of disulfiram concentrations. Metabolites of disulfiram do not interfere in this assay.
R, Fried, A N, Masoud, F M, Klein
openaire +2 more sources
Colorimetric assay for cellular transglutaminase
Analytical Biochemistry, 1989A colorimetric assay for cellular transglutaminase using 5-(biotinamido)pentylamine and polyvinylidine difluoride membranes for crude cellular preparations and purified enzyme has been developed. The biotinpentylamine substrate was incorporated into N,N-dimethylcasein by transglutaminase, the biotinylated products were adsorbed onto the membrane disks ...
W M, Jeon +4 more
openaire +2 more sources
Automated colorimetric assay of Norgestrel
Steroids, 1970Abstract A relatively sensitive assay for the contraceptive steroid norgestrel, in pharmaceutical preparations, is described. The procedure involves the blue tetrazolium reaction. Optimum conditions for color development were established. The relative standard deviation for the assay, which has a sample rate of 30 hr−1, were of the order of 0.9% at a
P M, Short, C T, Rhodes
openaire +2 more sources
Colorimetric assay of catalase
Analytical Biochemistry, 1972A simple colorimetric assay for catalase activity has been described using K2Cr2O7/acetic acid reagent. Kat. f values of different enzyme sources were determined by the colorimetric method and compared with the values obtained by titrimetric methods.
openaire +2 more sources
An automated colorimetric mutarotase assay
Analytical Biochemistry, 1966Abstract 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
openaire +2 more sources
Colorimetric Assay of Tetracycline Antibiotics
Journal of Pharmaceutical Sciences, 1971A 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
openaire +2 more sources
Detection of opines by colorimetric assay
Analytical Biochemistry, 1987A colorimetric procedure for confirming the presence of arginine-derived opines (nopaline and octopine) in plant tissue extracts is described. Those materials are widely used as markers of plant cell transformation and tumorigenesis mediated by the tumor-inducing plasmids of Agrobacterium tumefaciens.
N S, Yang, S G, Platt, P, Christou
openaire +2 more sources
An improved colorimetric assay for polyols
Analytical Biochemistry, 1977Abstract A new assay for polyols was developed that minimizes interference by sugars. It is based on oxidation of alditols to formaldehyde by acidic periodate, reduction of the excess periodate with l -rhamnose, and a short-time determination of the formaldehyde with the Nash reagent. When glycerol was added to various crude biological materials and
S H, Bok, A L, Demain
openaire +2 more sources
An easy colorimetric assay for glycosyltransferases
Biochemistry (Moscow), 2010Glycosyltransferases are involved in biosynthesis of both protein-bound and non-bound glycans that have multiple and important biological functions in all species. A variety of methods for assaying glycosyltransferase activity have been developed driven by the specific interests and type of information required by researchers.
Rui, Shen +6 more
openaire +2 more sources

