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maintained at a minimal value, or a large number of bracketing MW standards should be employed to de ne the shape of the calibration curve. 10.5. IDENTIFICATION OF ISOENZYMES Isoenzymes are enzymes from different species, or produced by different mechanisms within the same species, that catalyze identical reactions. Isoenzymes often differ from each other by only a few amino acid residues, and may have very similar molecular weights. In some cases, charged amino acid residues in one isoenzyme (e.g., lysine, arginine, aspartate, glutamate) may be substituted by uncharged amino acid residues in another, and this type of substitution will result in different net charges at a given pH, and different pI values for the different isoenzymes. For example, human alcohol dehydrogenase exists in more than twenty forms.6 These isoenzymes are all dimers, and all have molecular weights of $ 80 kDa, or $ 40 kDa per subunit. The different subunits have been called the a, b, g1, g2, p, and X subunits. All of the isoenzymes catalyze the conversion of ethanol to acetaldehyde according to Eq. 10.1: CH3 CH2 OH NAD ! CH3 CHO NADH H
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alcohol dehydrogenase
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Human alcohol dehydrogenase isoenzymes have been divided into three classes. Class I isoenzymes contain a, b, g1, and g2 subunit isoenzymes, are cationic at neutral pH, and are strongly inhibited by substituted pyrazole inhibitors. Class II isoenzymes contain the p isoenzyme subunit, are cationic at neutral pH, and are relatively insensitive to pyrazole inhibition. Class III isoenzymes contain the X subunit, are anionic at neutral pH and are insensitive to pyrazole inhibitors.
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Figure 10.5. Electrophoretic separation of the subunits of puri ed ADH isoenzymes in the presence of 7 M urea. Lane 1 contains Class II ADH, with only p subunits, while the Class I isoenzymes in lanes 2 7 have subunit compositions as indicated in each lane.
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DIAGNOSIS OF GENETIC (INHERITED) DISEASE
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Classes I and II have been studied using PAGE, with 7 M urea in the sample solution and gel, and with 10-mM dithiothreitol in the sample.7 The urea interferes with hydrogen bonding and unfolds the protein, while DTT reduces the disul de bonds. Because Class I and II isoenzymes are cationic at neutral pH, the samples are introduced at the anode and will migrate toward the cathode. While the masses of the different subunits are essentially identical, their net charges are signi cantly different, and this affects the charge/mass ratios that control electrophoretic mobilities. Figure 10.5 shows the stained gels obtained after a series of Class I and II alcohol dehydrogenase isoenzymes have been run. 10.6. DIAGNOSIS OF GENETIC (INHERITED) DISEASE The DNA diagnostic techniques generally use analyte DNA that has been isolated from white blood cells. This high molecular weight DNA may be digested with restriction endonucleases to yield shorter, double-stranded fragments. The fragments are separated on agarose gels, transferred to nylon or nitrocellulose membranes, and examined for the sequence of interest using labeled DNA probes. Restriction enzymes recognize certain regions, or sequences, of the DNA. These are relatively short, and occur at multiple sites over the entire native genome. Some examples of restriction enzymes and their recognition sites are listed in Table 10.3. Cleavage of the double-stranded DNA occurs where the slashes (/) are shown in the recognition sequence. The names of the restriction enzymes are derived from the species from which they are isolated (e.g., Eco is E. coli) and contain further classi cation numbers. The size of the recognition site of a restriction endonuclease may vary between 4 and 9 (or more) base pairs. A small site leads to multiple cleavages and many fragments, since this small site is statistically likely to occur more often, while larger recognition sites lead to fewer fragments. Sickle-cell anemia is a recessive genetic disorder that results from a single-base substitution, or a point mutation, in the gene that codes for the b-globin sequence of tetrameric human hemoglobin. This point mutation results in the substitution of one amino acid in the entire b-globin
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TABLE 10.3. Examples of Restriction Endonucleases and Their Recognition Sites Enzyme Sca I Hind III Eco RI Alu I Recognition Site 50 -AGT/ACT-30 30 -TCA/TGA-50 50 -A/AGCTT-30 30 -TTCGA/A-50 50 -G/AATTC-30 30 -CTTAA/G-50 50 -AG/CT-30 30 -TC/GA-50
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