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Hemoglobin, determination

Determine hemoglobin concentrations to the nearest 0.1 gdl-1 on the supemate (plasma). [Pg.401]

Heparinized blood 300 pi blood+300 pi digitonin 50% determine hemoglobin (Hb) concentration in the mix. [Pg.422]

A 100-pi aliquot of thawed erythrocytes is mixed well with 900 pi hemolysis buffer. This diluted hemolysate is used to determine hemoglobin concentration (e.g., by a routine technique). [Pg.776]

E246 Burdick, B.A., Hilbom, D.A. and Wu, T.W. (1986). A multilayer element for determining hemoglobin in whole blood Principles and analytical performance. Clin. Chem. 32, 1953-1955. [Pg.284]

Von Schenck H, Falkensson M, Lundberg B. Evaluation of HemoCue, a new device for determining hemoglobin. Clin Chem 1986 32 562-9. [Pg.320]

The sacroplasmic proteins myoglobin and hemoglobin are responsible for much of the color in meat. Species vary tremendously in the amount of sacroplasmic proteins within skeletal muscle with catde, sheep, pigs, and poultry Hsted in declining order of sarcoplasmic protein content. Fat is also an important component of meat products. The amount of fat in a portion of meat varies depending on the species, anatomy, and state of nutrition of the animal. The properties of processed meat products are greatiy dependent on the properties of the fat included. Certain species, such as sheep, have a relatively higher proportion of saturated fat, whereas other species, such as poultry, have a relatively lower proportion of saturated fat. It is well known that the characteristic davors of meat from different species are in part determined by their fat composition. [Pg.32]

AH of the reactions considered to be useful in the production of hemoglobin-based blood substitutes use chemical modification at one or more of the sites discussed above. Table 2 Hsts the different types of hemoglobin modifications with examples of the most common reactions for each. Differences in the reactions are determined by the dimensions and reactivity of the cross-linking reagents. Because the function of hemoglobin in binding and releasing... [Pg.162]

Figure 3.13 The hemoglobin molecule is built up of four polypeptide chains two a chains and two (3 chains. Compare this with Figure 1.1 and note that for purposes of clarity parts of the a chains are not shown here. Each chain has a three-dimensional structure similar to that of myoglobin the globin fold. In sicklecell hemoglobin Glu 6 in the (3 chain is mutated to Val, thereby creating a hydrophobic patch on the surface of the molecule. The structure of hemoglobin was determined in 1968 to 2.8 A resolution in the laboratory of Max Perutz at the MRC Laboratory of Molecular Biology, Cambridge, UK. Figure 3.13 The hemoglobin molecule is built up of four polypeptide chains two a chains and two (3 chains. Compare this with Figure 1.1 and note that for purposes of clarity parts of the a chains are not shown here. Each chain has a three-dimensional structure similar to that of myoglobin the globin fold. In sicklecell hemoglobin Glu 6 in the (3 chain is mutated to Val, thereby creating a hydrophobic patch on the surface of the molecule. The structure of hemoglobin was determined in 1968 to 2.8 A resolution in the laboratory of Max Perutz at the MRC Laboratory of Molecular Biology, Cambridge, UK.
FIGURE 15.29 The arrangement of snbnnits in horse methemoglobin, the first hemoglobin whose strnctnre was determined by X-ray diffraction. The iron atoms on metHb are in the oxidized, ferric (Fe ) state. (Irving Gets)... [Pg.484]

We can determine quantitatively the physiological significance of the sigmoid nature of the hemoglobin oxygen-binding curve, or, in other words, the biological importance of cooperativity. The equation... [Pg.484]

WEB The molar mass of a type of hemoglobin was determined by osmotic pressure measurement A student measured an osmotic pressure of 4.60 mm Hg for a solution at 20°C containing 3.27 g of hemoglobin in 0.200 L of solution. What is the molar mass of hemoglobin ... [Pg.281]

Some of the abnormal fetal hemoglobin variants are the product of an allele of the structural locus and others of an allele of the % structural locus The structural abnormality In all eight variants of Hb-A2 has been determined ... [Pg.7]

Hematological Methods. Hematological analyses can Include the determination of the total hemoglobin concentration (In g%), the packed cell volume (PCV In %), the red blood cell count (In 10 /mm ) and reticulocytes count (In %), calculation of the red cell Indices, examination of a blood film, tests to demonstrate the presence of Inclusion bodies and of sickle cells, tests to evaluate the distribution of fetal hemoglobin (Hb-F) Inside the red cells, the red cell osmotic fragility, the concentration of serum Iron (SI), total Iron binding capacity (TIBC), and the survival time of the red cells. Details of all... [Pg.9]

Mlcrochromatographlc Methods During the past two years rapid. Inexpensive, miniaturized column chromatographic methods for the separation of hemoglobins have been developed These methods are designed for the qualitative detection and quantitative determination of hemoglobins In normal and abnormal conditions and cover the quantitation of Hb-A2 the detection of Hb-S, Hb-C other abnormal Hbs differentiation of various conditions In adults and the detection of hemoglobinopathies especially sickle cell anemia at birth (27, 28, 29, 30) ... [Pg.18]

The Determination of Fetal Hemoglobin (Hb-F). Specific properties of Hb-F have given rise to various methods for Its detection and quantitation which are based on electrophoretic and chromatographic mobilities of Hb-F, on Its slow rate of... [Pg.24]

Thus, the determination of the content of Isoleuclne In relation to leucine and phenylalanine can be used as a measure of the relative amount of Hb-F In mixtures. The procedure Involves the chromatographic Isolation of the Hb-F containing zone and the determination of the Isoleucyl, and phenylalanyl content In a 72 hour acid hydrolysate of the hemoglobins In this zone. [Pg.26]

Detection of Variants With Altered Functional Properties. When substitutions In either a-or 3-chains Involve amino acid residues that participate In the contact with heme or the contact between chains, changes In functional properties can occur and the determination of the oxygen affinity of the blood sample or of an Isolated hemoglobin variant Is desirable. Oxygen affinity Is affected by temperature, pH, salt concentration, the level of 2,3-dlphosphoglycerate (2,3-DPG), and to a lesser extent by the concentration of the hemoglobin. The concentration of 2,3-DPG In blood changes rather rapidly after collection and a... [Pg.30]


See other pages where Hemoglobin, determination is mentioned: [Pg.274]    [Pg.267]    [Pg.89]    [Pg.220]    [Pg.3]    [Pg.1175]    [Pg.259]    [Pg.545]    [Pg.465]    [Pg.4174]    [Pg.272]    [Pg.274]    [Pg.267]    [Pg.89]    [Pg.220]    [Pg.3]    [Pg.1175]    [Pg.259]    [Pg.545]    [Pg.465]    [Pg.4174]    [Pg.272]    [Pg.551]    [Pg.330]    [Pg.201]    [Pg.338]    [Pg.400]    [Pg.400]    [Pg.403]    [Pg.2]    [Pg.320]    [Pg.178]    [Pg.526]    [Pg.688]    [Pg.99]    [Pg.578]    [Pg.158]    [Pg.817]    [Pg.891]    [Pg.82]    [Pg.1]    [Pg.30]    [Pg.19]    [Pg.34]    [Pg.46]   
See also in sourсe #XX -- [ Pg.153 ]




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