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Hemoglobin assays

Fig. 10.5 NO formation from the oxidation of N-al kyl-N -hyd roxyguan id ines in the presence of NOS. The reaction rates were assessed by a hemoglobin assay and are expressed as a percentage of those of NHA. Fig. 10.5 NO formation from the oxidation of N-al kyl-N -hyd roxyguan id ines in the presence of NOS. The reaction rates were assessed by a hemoglobin assay and are expressed as a percentage of those of NHA.
Although many different procedures have been described for preparation prior to glycosylated hemoglobin assay, a standard method applicable to... [Pg.14]

These rapid and simple techniques (short column, centrifiigation, batch separation), with reusable supplies and equipment, are cost-effective and provide reasonable accuracy, provided that sources of variation are rigidly controlled. In final analysis, accuracy is to be preferred over rapidity and low cost. Glycosylated hemoglobin assays, in contrast to frequent or daily blood glucose determinations, are only required once every 4-12 weeks for diabetic control surveillance. [Pg.18]

Intermediate Monitor. Glycosylated (ketoamine) hemoglobin assays provide an overview of control for the previous 5 to 8 weeks. Such assays are independent of patient compliance an assay every 2 to 3 months will also reduce the number of blood samplings required for blood glucose estimation. [Pg.48]

D17. Dods, R. F., and Bolraey, C., Glycosylated hemoglobin assay and oral glucose tolerance test compared for detection of diabetes mellitus. Clin. Chem. 25, 764-768 (1979). [Pg.61]

Hemoglobin assay. Pepsin activity was determined by the method of Chow and Kassel1 (20). [Pg.161]

One incubation cycle was for 30 min, and additional substrate solution was added at 30 min intervals for multiple incubation experiments. At the end of the experiments, the enzyme solution was dialyzed at 4° against five changes of 3 1 of 0.01 M sodium acetate, pH 4.0, for a total of 72 hr. Measurements of peptic activity by the hemoglobin assay method and the quantitative analysis of hydroxamic acid were performed as mentioned above. [Pg.161]

Blanking Schemes. Whereas most clinical assays rely on the specificity of the assay reaction to avoid interferences that would require a blank correction, certain ubiquitous interferences, eg, lipemic turbidity, hemoglobin in hemoly2ed sera, bilinibin [635-65-4] in icteric specimens,... [Pg.393]

After in vivo administration in rats TDA induced formation of both DNA and hemoglobin adducts in a dose-dependent manner. TDA was mutagenic in bacterial assays. ... [Pg.208]

Brydon and Roberts- added hemolyzed blood to unhemolyzed plasma, analyzed the specimens for a variety of constituents and then compared the values with those in the unhemolyzed plasma (B28). The following procedures were considered unaffected by hemolysis (up to 1 g/100 ml hemoglobin) urea (diacetyl monoxime) carbon dioxide content (phe-nolphthalein complex) iron binding capacity cholesterol (ferric chloride) creatinine (alkaline picrate) uric acid (phosphotungstate reduction) alkaline phosphatase (4-nitrophenyl phosphate) 5 -nucleotidase (adenosine monophosphate-nickel) and tartrate-labile acid phosphatase (phenyl phosphate). In Table 2 are shown those assays where increases were observed. The hemolysis used in these studies was equivalent to that produced by the breakdown of about 15 X 10 erythrocytes. In the bromocresol green albumin method it has been reported that for every 100 mg of hemoglobin/100 ml serum, the apparent albumin concentration is increased by 100 mg/100 ml (D12). Hemolysis releases some amino acids, such as histidine, into the plasma (Alb). [Pg.5]

S.A. = 0.67 in octyl glucoside buffer) could be found in all of the detergent-extract preparations. As above, the hemoglobin step increased dramatically the S.A. of shikimate dehydrogenase assayed in detergent-extract preparations. [Pg.96]

K-Assay LPO-CC Oxidation by lipid hydroperoxides of a derivative of the leuco form of Methylene Blue (90) to the colored form (91), catalyzed by hemoglobin, according to equation 29 measurement is at 675 nm . e... [Pg.632]

Eaton, D.L. and Toal, B.F. (1982). Evaluation of the Cd hemoglobin affinity assay for the rapid determination of metal-lothionein in biological tissues. Toxicology and Applied Pharmacology, 66 134-142. [Pg.127]


See other pages where Hemoglobin assays is mentioned: [Pg.264]    [Pg.265]    [Pg.943]    [Pg.26]    [Pg.26]    [Pg.47]    [Pg.54]    [Pg.55]    [Pg.70]    [Pg.73]    [Pg.264]    [Pg.265]    [Pg.943]    [Pg.26]    [Pg.26]    [Pg.47]    [Pg.54]    [Pg.55]    [Pg.70]    [Pg.73]    [Pg.201]    [Pg.393]    [Pg.260]    [Pg.264]    [Pg.284]    [Pg.319]    [Pg.970]    [Pg.24]    [Pg.46]    [Pg.234]    [Pg.282]    [Pg.271]    [Pg.73]    [Pg.96]    [Pg.208]    [Pg.224]    [Pg.271]    [Pg.350]    [Pg.505]    [Pg.535]    [Pg.329]    [Pg.7]    [Pg.260]    [Pg.305]    [Pg.317]   
See also in sourсe #XX -- [ Pg.264 ]




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