A hemoglobin

Positive-ion electrospray mass spectrum of human hemoglobin (a) as initially obtained with all the measured masses, and (b) after calculation of true mass, as in Figure 8.3. The spectrum transforms into two main peaks representing the main alpha and beta chains of hemoglobin with accurate masses as given. This transformation is fnlly automated. The letters A, B, C refer to the three chains of hemoglobin. Thus, A13 means the alpha chain with 13 protons added. 

Carbon monoxide seriously impedes transport of oxygen. The deadly effect of inhaled CO results from its reaction with hemoglobin. A CO molecule is almost the same size and shape as O2, so it fits into the binding pocket of the hemoglobin molecule. In addition, the carbon atom of CO forms a stronger bond to than does O2. Under... 

Two sets of samples have been analyzed on one plate with a standard mixture of the hemoglobins C, S, A, and F occupying the fourth position from the ton. The data show that the hemoglobins A, F, S, and C are readily separated that the hemoglobins E and Dp do not separate from Hb-A and that some p-chain variants can readily be separated from Hb-F, Hb-A, Hb-S. or Hb-C (examples are the unidentified Hb-J, Hb-Fort Gordon (see also Figure 14), and Hb-O-Arab). 

Shikama K. 1998. The molecular mechanism of autoxidation for myoglobin and hemoglobin A venerable puzzle. Chem Rev 98 1357. 

Sickle hemoglobin A defective form of hemoglobin produced as a result of a single substitution of the amino acid valine for glutamic acid at position 6 of the (1-polypeptide chain. 

The letter N indicates that any nucleotide at that position satisfies the specificity of Mstll. The normal sequence of the DNA of the 13-chain of hemoglobin A near the site of the sickle cell mutation is . ..C-C T-G-A-G-G. 

Restriction analysis can be used to detect sickle cell disease prenatally, since the DNA of all cells, including amniotic cells, carries the mutant DNA. It is much more difficult to obtain fetal blood for the analysis of the mutant hemoglobin A P-chain. Furthermore, fetal blood is composed mostly of fetal hemoglobin, sinee-hemoglobin A is made later in development. 

Simon, S.R., and Konigsberg, W.H. (1966) Chemical modification of hemoglobins A study of conformation restraint by internal bridging. Proc. Natl. Acad. Sci. USA 56, 749. 

The information of Tables 4.3 and 4.4 indicates that a water molecule is found in the binding cavity of a chains of hemoglobin A (HbA) even though this cavity has been called hydrophobic. Indeed, although many hydrophobic groups such as... 

Clinical tests are targeted to measure the concentration of different sets of compounds, such as small molecules (e.g., amino acids, fatty acids, organic acids, steroids) and peptides and proteins (e.g., thyroid stimulating hormone, hemoglobin A 1C) and oligonucleotides (e.g., DNA, RNA, SNPs). The presence, absence, or altered concentrations of a diagnostic compound or compounds may indicate the presence of a disease, type and severity of a disease, risk factors for disease, what is the basis for... 

Dll. Drabkin, D. L., Maintenance of active hemoglobin, a function of erythrocytes. Federation Froc. 5, 132 (1946). 

HCN in the blood is almost completely contained in the red blood cells where it is bound to methemoglobin. Immediately after infusion of sodium nitroprusside into patients, 98.4% of the blood cyanide was found in the red blood cells (Vesey et al. 1976). At normal physiological levels of body methemoglobin (0.25% to 1% of the hemoglobin), a human adult can bind about 10 mg of HCN (Schulz 1984). 

Hemoglobin (a) Trauma (b) Surgery Polycythemia Polycythemia (increase in Anemias... 

Fig. 3.16. 3D Representation of the esterase site in hemoglobin A (oxy-Hb A, modified from...

Figure 8.5 Effect of pH on protein mobility. Hemoglobin A (pi 7.1) and Hemoglobin C (pi 7.4) were electrophoresed in eight of the McLellan native, continuous buffer systems (Table 8.1). The diagram is drawn to scale. Migration is from top to bottom as shown by the vertical arrows. Bands marked A or C indicate the positions of the two hemoglobin variants in each gel representation. The polarities of the voltages applied to the electrophoresis cell are indicated by + and - signs above and below the vertical arrows. Run times are shown below the arrows. Note the polarity change between the gel at pH 7.4 and the one at pH 8.2. This reflects the pis of the two proteins (and was accomplished by reversing the leads of the electrophoresis cell at the power supply).

Table 9.2 Migration Time and Isoelectric Point Reproducibility for Human Hemoglobins A and S Analyzed by CIEF...

Fig. 4. C-terminal salt bridges and the role of the residue F9j8 in the T and R structures of mammalian and fish hemoglobins, (a) Human T structure (b) human R structure (c) carp T structure (d) carp R structure. The letters F, G, and H denote helical segments FG, GH, and HC denote nonhelical segments. The same notation is used in Fig. 5 (23).

Linked Functions and Reciprocal Effects in Hemoglobin A Second Look Jeffries Wyman, Jr. 

Brucker EA. Genetically crosslinked hemoglobin a structural study. Acta Crys-tallogr D Biol Crystallogr 2000 56(Pt 7) 812. 

Phillips W, Klipper R, Awasthi V, et al. Polyethylene glycol-modified liposome-encapsulated hemoglobin a long circulating red cell substitute. J Pharmacol Exp Ther 1999 288 665. 

Farmer MC, Johnson SA, Beissinger RL, et al. Liposome-encapsulated hemoglobin a synthetic red cell. Adv Exp Med Biol 1988 238 161. 

Rudolph AS. The freeze-dried preservation of liposome encapsulated hemoglobin a potential blood substitute. Cryobiology 1988 25 277. 

Rudolph AS, Cliff RO. Dry storage of liposome-encapsulated hemoglobin a blood substitute. Cryobiology 1990 27 585. 

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