activating regulator mutations Analysis of amino acid sequence data from the alpha and beta hemoglobins and myoglobins suggests that the gene lineages deviate relatively little from established species relationships, and that most contemporary gene pairs in this phylogenetic system may be regarded as orthologous (split at the time of speciation) rather than paralogous (split prior to speciation) It also appears that as the statistical sample of orthologous sequence sites becomes greatly enlarged by tandem alignment of enough different types of protein chains, the parsimony reconstruction based strictly on minimal nucleotide replacement length will itself reveal the correct cladogram for the set of contemporary species [Phylogeny reconstruction; parsimony methods; globin sequences; gene phylogeny; species phylogeny]

https://www.jstor.org/stable/pdfplus/2412519.pdf

Fitting the Gene Lineage into its Species Lineage, a Parsimony Strategy Illustrated by Cladograms Constructed from Globin Sequences

Diseases affecting hemoglobin synthesis and function are extremely common worldwide. More than 1000 naturally occurring human hemoglobin variants with single amino acid substitutions throughout the molecule have been discovered, mainly through their clinical and/or laboratory manifestations. These variants alter hemoglobin structure and biochemical properties with physiological effects ranging from insignificant to severe. Studies of these mutations in patients and in the laboratory have produced a wealth of information on hemoglobin biochemistry and biology with significant implications for hematology practice. More generally, landmark studies of hemoglobin performed over the past 60 years have established important paradigms for the disciplines of structural biology, genetics, biochemistry, and medicine. Here we review the major classes of hemoglobin variants, emphasizing general concepts and illustrative examples.

/pdf/hemoglobin-variants-biochemical-properties-and-clinical-1ufzjaelyt.pdf

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Letter: Reference: references.

An ancestral myoglobin chain has been deduced by comparing the differences in the amino acid sequences of eighteen living species and assessing from the fossil evidence the probable times of divergence of their ancestors.

Molecular Evolution of Myoglobin and the Fossil Record: a Phylogenetic Synthesis

A prolonged sojourn above 5500 m induces muscle deterioration and accumulation of lipofuscin in Caucasians, probably because of overproduction of reactive oxygen species (ROS). Because Sherpas, who live at high altitude, have very limited muscle damage, it was hypothesized that Himalayan natives possess intrinsic mechanisms protecting them from oxidative damage. This possibility was investigated by comparing the muscle proteomes of native Tibetans permanently residing at high altitude, second-generation Tibetans born and living at low altitude, and Nepali control subjects permanently residing at low altitude, using 2D gel electrophoresis and mass spectrometry. Seven differentially regulated proteins were identified: glutathione-S-transferase P1-1, which was 380% and 50% overexpressed in Tibetans born and living at high and low altitude, respectively; Delta2-enoyl-CoA-hydratase, which was up-regulated in both Tibetan groups; glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase, which were both slightly down-regulated in Tibetans born and living at high altitude; phosphoglycerate mutase, which was 50% up-regulated in the native Tibetans; NADH-ubiquinone oxidoreductase, slightly overexpressed in Tibetans born and living at high altitude; and myoglobin, which was overexpressed in both Tibetan groups. We concluded that Tibetans at high altitude, and to some extent, those born and living at low altitude, are protected from ROS-induced tissue damage and possess specific metabolic adaptations.

New aspects of altitude adaptation in Tibetans: a proteomic approach

Summary: A new unstable haemoglobin, Hb Peterborough, is described in father and son. In the former it was found with Hb A but in the latter with Hb Lepore, the mother being a heterozygote for Hb A and Hb Lepore Boston (or Washington). In this respect it differs from other unstable haemoglobins so far described which have been observed in heterozygotes together with normal adult haemoglobin. It was therefore possible to compare the clinical and biochemical interactions of Hbs A and Peterborough, A and Lepore, and Peterborough and Lepore.



Hb Peterborough has been identified as βiii (G-13) Val Phe. It has a low oxygen affinity, but the Bohr effect and haem-haem interaction appear to be normal.

An unstable haemoglobin with reduced oxygen affinity: haemoglobin Peterborough, 3 (GI3) Valine lead to Phenylalanine, its interaction with normal haemoglobin and with haemoglobin Lepore.

H. Lehmann

Papers

An unstable haemoglobin with reduced oxygen affinity: haemoglobin Peterborough, 3 (GI3) Valine lead to Phenylalanine, its interaction with normal haemoglobin and with haemoglobin Lepore.

Haemoglobin bucureşti β42 (CD1) Phe → Leu, a cause of unstable haemoglobin haemolytic anaemia

The myoglobin of primates. I. Hylobates agilis (gibbon).

HaemoglobinDhofar — A new variant from Southern Arabia

Haemoglobin Denmark Hill α95 (G2) Pro-Ala, a variant with unusual electrophoretic and oxygen-binding properties