Glyoxalase-I (EC 4.4.1.5) is polymorphic in humans but not in the closely related hominoid species, Pan troglodytes (the common chimpanzee). The electrophoretic mobility of chimpanzee glyoxalase-I is identical to that of human GLO2, as is that of another Old World primate, Macaca fasicularis. These evidences suggest that GLO2 may be the ancestral allele at this locus in hominoids. The significance of the human GLO variation is discussed in the light of other recent findings showing balanced polymorphism at this locus.

Alleles↗

PubMed1981

The untranslated regions of beta-globin mRNA evolve at a functional rate in higher primates.

We have sequenced the 3' and 5' untranslated regions of beta-globin mRNAs from cebus monkey, rhesus monkey and chimpanzee. A comparison with the corresponding human sequences reveals that the rate of sequence divergence among the higher primates is the same in the 3' and 5' noncoding regions and that this rate is several times lower than the rate for silent substitutions in the coding regions. In addition, the rate of sequence divergence in the 3' untranslated region of the primate beta-globin nRNA is several times lower than the rate calculated for this region from other comparisons. The low rate of sequence divergence in the noncoding 3' end of the primate beta-globin mRNAs may indicate a specialized and significant function for this region in the higher primates.

Animals↗

PubMed1981

Studies on the active site of pig kidney aldehyde reductase.

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Alcohol Oxidoreductases↗

PubMed1981

Extensive polymorphism in the mitochondrial DNA of apes.

Ape species are 2-10 times more variable than the human species with respect to the nucleotide sequence of mtDNA, even though ape populations have been smaller than the human population for at least 10,000 years. This finding was made by comparing purified mtDNAs from 27 individuals with the aid of 25 restriction endonucleases; for an additional 59 individuals, comparisons were made with fewer enzymes by using the blot hybridization method. The amount of intraspecific sequence divergence was greatest between orangutans of Borneo and Sumatra. Among common chimpanzees, a large component of the variation is due to two highly distinct forms of mtDNA that may reflect a major geographic subdivision. The least amount of sequence variation occurred among lowland gorillas, which exhibit only twice as much sequence variation as humans. The large intraspecific differences among apes, together with the geological and protein evidence, leads us to propose that each ape species is the remnant of an ancient and widespread population that became subdivided geographically and reduced in size and range, perhaps by hominid competition. The low variation among human mtDNAs is consistent with geological evidence that the human species is young. The distribution of site changes within the mitochondrial genome was also examined. Comparison of closely related mtDNAs shows that the ribosomal RNA genes have diverged more slowly than the rest of the genome.

Animals↗

PubMed1980

Evolution of aldehyde reductase: an immunological approach to the relatedness of aldehyde reductase from different species.

Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Aves indicating considerable differences in the amino acid sequences of the aldehyde reductase of these species. Immunological distances for aldehyde reductase between pairs of insect species or bird species when plotted against the immunological distances for transferrin, albumin, lysozyme and alpha-glycerophosphate dehydrogenase for the same pairs of species gave a linear relationship in each case. From these relationships the rate of evolution of aldehyde reductase in terms of a unit evolutionary period (UEP) was calculated to be 12 which agreed favorably with the value previously obtained from compositional comparisons. A UEP of 12 is approximately half that of lactate dehydrogenase and shows that aldehyde reductase is evolving at twice the rate of glycolytic enzymes. This may indicate a relatively non-essential metabolism role for the enzyme.

Aldehyde Oxidoreductases↗

PubMed1979

A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney.

Pig kidney aldehyde reductase is inactivated by 2,3-butanedione, phenylglyoxal, methylglyoxal, and 1,2-cyclohexanedione. 2,3-Butanedione caused the most rapid loss in enzyme activity, the rate of loss being proportional to the concentration of 2,3-butanedione. Neither D-glyceraldehyde nor pyridine 3-aldehyde, both substrates for this broadly specific enzyme, protected the enzyme from inactivation but 1 mM NADPH or NADP completely prevented the loss of activity by 2,3-butanedione suggesting the involvement of arginine in the binding of cofactor. Nicotinamide mononucleotide (NMN) (reduced form) offered no protection to inactivation whereas ADP-ribose phosphate gave complete protection indicating that it is the latter portion of NADPH which interacts with the essential arginine. Both NMN and ADP-ribose phosphate are competitive inhibitors of aldehyde reductase with respect to NADPH. Butanedione-modified aldehyde reductase could still bind to a blue dextran-Sepharose 4B column suggesting that the modified arginine did not bind NADPH. This was confirmed by fluorescence spectra which showed that chemically modified aldehyde reductase caused the same blue shift of NADPH fluorescence as did native aldehyde reductase. Of additional interest was the quenching of NADPH fluorescence by aldehyde reductase which, with one exception, is in contrast to the fluorescence behavior of all other oxidoreductases.

Aldehyde Oxidoreductases↗

PubMed1979

Kinetics and mechanism of action of aldehyde reductase from pig kidney.

An improved procedure for purifying aldehyde reductase is described. Utilization of Blue Dextran--Sepharose 4B and elimination of hydroxyapatite chromatography greatly improves the yield and ease of purification. Starting with 340 g of kidney tissue (two pig kidneys) approx. 50 mg of purified reductase may be routinely and reproducibly obtained. The purified reductase was used to establish the kinetic reaction mechanism of the enzyme. Initial-velocity analysis and product-inhibition data revealed that pig kidney aldehyde reductase follows an Ordered Bi Bi reaction mechanism in which NADPH binds first before D-glyceraldehyde. The limiting Michaelis constants for D-glyceraldehyde and NADPH were 4.8 +/- 0.7 mM and 9.1 +/- 2.1 micrometer respectively. The mechanism is similar to that of another monomeric oxidoreductase, octopine dehydrogenase, towards which aldehyde reductase exhibits several similarities, but differs from that of other aldehyde reductases. Phenobarbital is a potent inhibitor of aldehyde reductase, inhibiting both substrate and cofactor non-competitively (Ki = 80.4 +/- 10.5 micrometer and 66.9 +/- 1.6 micrometer respectively). Barbiturate inhibition seems to be a common property of NADPH-dependent aldehyde reductases.

Aldehyde Oxidoreductases↗

PubMed1979

Compositional relatedness of aldehyde reductases from several species.

The amino acid compositions of several monomeric NADPH-dependent aldehyde reductases from a variety of species have been determined and analyzed by the difference index method of Metzger et al. (1968). The difference indexes among mammals range from 4.15 - 6.10 indicating considerable homology. Comparison of chicken aldehyde reductase with mammalian aldehyde reductases gave values in the range 6.8 - 9.9 suggesting a close relationship whereas the difference indexes for the enzymes from fruit fly and Baker's yeast versus vertebrate aldehyde reductases (10.9 - 14.4) indicate more distant relationships. The extent of sequence homology among aldehyde reductases from these species was estimated from a plot of difference index versus percent sequence difference for oxido-reductases of known sequence. From this plot, and using a mammal-chicken divergence time of 300 million years and a mammalian order split of 75 million years, the rate of evolution of aldehyde reductases was calculated to lie in the range 5.8 - 15.6% sequence difference per 100 million years. Comparison with rates of evolution of oligomeric dehydrogenases indicates that aldehyde reductases comprise the most rapidly evolving family of oxido-reductases. This is probably related to the monomericity of aldehyde reductases since there is a direct correlation between the number of subunits and the rate of evolution.

Aldehyde Oxidoreductases↗

PubMed1978

Do we really want a program evaluation strategy based solely on individualized goals? A critique of goal attainment scaling.

Goal attainment scaling is a program evaluation technique that measures program success using individualized client goals rather than the same measuring instrument for all clients. Although the reliability of the goal attainment scales is generally acceptable, such scales have not exhibited satisfactory validity. Also when clients have not been assigned to programs randomly, evaluations comparing two or more programs using goal attainment scales are potentially more biased than evaluations that use the same outcome measure for all clients. Thus since goal attainment scaling does have therapeutic value, program evaluators should adopt a multivariate assessment strategy combining goal attainment scaling with uniform measuring instruments.

Community Mental Health Services↗

PubMed1978

A comparative study of the tissue and species distribution of NADPH-dependent aldehyde reductase.

1. NADPH-dependent aldehyde reductase (AR) is widely distributed among animal species. It also occurs in flowering plants and fungi (yeast). 2. AR is located mainly in the kidney or renal tissue of all species examined, with the exception of fish where it occurs mainly in the liver. 3. The enzyme from each species is monomeric and has a molecular weight between 30,000 and 40,000 daltons. 4. The enzymes exhibit similar substrate specificities and pH profiles and are inhibited by barbiturates. 5. In the reduction of D-glyceraldehyde the monomeric AR of each species catalyzes the stereospecific transfer of the A hydrogen from NADPH.

Alcohol Oxidoreductases↗

PubMed1978