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At least 19 recordsLinked to original sources
PubMed1997

Evolutionary affinities of the order Perissodactyla and the phylogenetic status of the superordinal taxa Ungulata and Altungulata.

Contrary to morphological claims, molecular data indicate that the order Perissodactyla (e.g., horses, rhinoceroses, and tapirs) is neither part of the superordinal taxon Paenungulata (Sirenia, Proboscidea, and Hyracoidea) nor an immediate outgroup of the paenungulates. Rather, Perissodactyla is closer to Carnivora and Cetartiodactyla (Cetacea+Artiodactyla) than it is to the paenungulates. Therefore, two morphologically defined superordinal taxa, Altungulata (Proboscidea, Sirenia, Hyracoidea, and Perissodactyla) and Ungulata (Altungulata and Cetartiodactyla), are invalidated. Perissodactyla, Carnivora, and Cetartiodactyla are shown to constitute a rather tight trichotomy. However, a molecular analysis of 36 protein sequences with a total concatenated length of 7885 aligned amino acids indicates that Perissodactyla is closer to Cetartiodactyla than either taxa is to Carnivora. The relationships among Paenungulata, Primates, and the clade consisting of Perissodactyla, Carnivora, and Cetartiodactylaa could not be resolved on the basis of the available data.

Amino Acid Sequence↗
PubMed1996

The complete mitochondrial DNA sequence of the greater Indian rhinoceros, Rhinoceros unicornis, and the Phylogenetic relationship among Carnivora, Perissodactyla, and Artiodactyla (+ Cetacea).

The sequence (16,829 nt) of the complete mitochondrial genome of the greater Indian rhinoceros, Rhinoceros unicornis, was determined. Like other perissodactyls studied (horse and donkey) the rhinoceros demonstrates length variation (heteroplasmy) associated with different numbers of repetitive motifs in the control region. The 16,829-nt variety of the molecule includes 36 identical control region motifs. The evolution of individual peptide-coding genes was examined by comparison with a distantly related perissodactyl, the horse, and the relationships among the orders Carnivora, Perissodactyla, and Artiodactyla (+ Cetacea) were examined on the basis of concatenated sequences of 12 mitochondrial peptide-coding genes. The phylogenetic analyses grouped Carnivora, Perissodactyla, and Artiodactyla (+ Cetacea) into a superordinal clade and within this clade a sister group relationship was recognized between Carnivora and Perissodactyla to the exclusion of Artiodactyla (+ Cetacea) . On the basis of the molecular difference between the rhinoceros and the horse and by applying as a reference to Artiodactyl/Cetacean divergence set at 60 million years ago (MYA), the evolutionary divergence between the families Rhinocerotidae and Equidae was dated to approximately 50 MYA.

Animals↗
PubMed1993

Purification and characterization of insulin and the C-peptide of proinsulin from Przewalski's horse, zebra, rhino, and tapir (Perissodactyla).

Within the order Perissodactyla, the primary structure of insulin has been strongly conserved. Insulin from Przewalski's horse and the mountain zebra (suborder Hippomorpha) is the same as that from the domestic horse and differs from insulin from the white rhinoceros and mountain tapir (suborder Ceratomorpha) by a single substitution (Gly-->Ser) at position 9 in the A-chain. A second molecular form of Przewalski's horse insulin isolated in this study was shown to represent the gamma-ethyl ester of the Glu17 residue of the A-chain. This component was probably formed during the extraction of the pancreas with acidified ethanol. The amino acid sequence of the C-peptide of proinsulin has been less well conserved. Zebra C-peptide comprises 31 amino acid residues and differs from Przewalski's horse and domestic horse C-peptide by one substitution (Gln30-->Pro). Rhino C-peptide was isolated only in a truncated form corresponding to residues (1-23) of intact C-peptide. Its amino acid sequence contains three substitutions compared with the corresponding region of horse C-peptide. It is postulated that the substitution (Pro23-->Thr) renders rhino C-peptide more liable to proteolytic cleavage by a chymotrypsin-like enzyme than horse C-peptide. C-peptide could not be identified in the extract of tapir pancreas, suggesting that proteolytic degradation may have been more extensive than in the rhino. In contrast to the ox and pig (order Artiodactyla), there was no evidence for the expression of more than one proinsulin gene in the species of Perissodactyla examined.

Amino Acid Sequence↗
PubMed2000

Phylogenetics of Perissodactyla and tests of the molecular clock.

Two mitochondrial genes, the protein-coding cytochrome c oxidase subunit II (COII) gene and a portion of the 12S rRNA gene, were used for phylogenetic investigation of the mammalian order Perissodactyla. The primary objective of the study was to utilize the extensive fossil record of perissodactyls for calibrating molecular clocks and comparing estimates of divergence times using both genes and two fossil calibration points. Secondary objectives included clarification of previously unresolved relationships within Tapiridae and comparison of the results of separate and combined analyses of two genes. Analyses included several perissodactyl lineages representing all three families (Tapiridae, Equidae, and Rhinocerotidae), most extant genera, all four species of tapirs, two to four species of rhinoceros, and two species of Equus. The application of a relatively recent fossil calibration point and a relatively ancient calibration point produced greatly different estimates of evolutionary rates and divergence times for both genes, even though a relative rates test did not find significant rate differences among taxa. A likelihood-ratio test, however, rejected a molecular clock for both genes. Neither calibration point produced estimates of divergence times consistent with paleontological evidence over a range of perissodactyl radiations. The combined analysis of both genes produces a well-resolved phylogeny with Perissodactyla that conforms to traditional views of interfamilial relationships and supports monophyly of neotropical tapirs. Combining the data sets increases support for most nodes but decreases the support for a neotropical tapir clade because the COII and 12S rRNA data sets are in conflict for tapir relationships.

Animals↗
PubMed1979

Plasma lipids and lipoproteins of some members of the order Perissodactyla.

1. The plasma lipoproteins of various members of the order Perissodactyla have been examined by electrophoresis and analytical ultracentrifugation. 2. In the Equidae, high density (alpha) lipoprotein was the major component (80-90%) and low density (beta) lipoprotein (10-20%) the minor component. 3. In the Tapiridae represented by the Malayan tapir (Tapirus indicus), high density and low density lipoproteins were present in approximately equal amounts. 4. In the Rhinocerotidae, the high density lipoprotein characteristic of the Equidae and Tapiridae was absent, and the plasma lipoproteins consisted of a complex group having beta mobility on electrophoresis and a flotation pattern usually associated with low density lipoprotein. 5. The fatty acid composition of plasma lipids was remarkably similar in all members of the Perissodactyla examined, with very high percentages of linoleic acid (greater than 70%) being found in the cholesteryl esters.

Animals↗
PubMedDate not supplied

Origins of spondyloarthropathy in Perissodactyla.

OBJECTIVE: Spondyloarthropathy has clearly been documented as not limited in occurrence to humans. Transmammalian in nature, it is of interest to understand the antiquity, and perhaps the origins, of this disorder in animal groups sufficiently represented in the skeletal record. METHODS: Fossil and recent skeletons of perissodactylae from North America were systematically examined to determine the occurrence and population frequency of spondyloarthropathy. RESULTS: Spondyloarthropathy was the most common form of arthritis recognized in the extant and fossil records. Common in extinct families such as Brontotheriidae and Chalicotheriidae, a progressive increase in the frequency of spondyloarthropathy was observed through geologic time in Equidae and Rhinocerotidae. CONCLUSION: Erosive arthritis of the spondyloarthropathy variety is now documented as not only persisting in Perissodactyla, but as actually increasing significantly in frequency (3-6 fold). Given the unusual evolutionary penetrance of this "disease," the possibility must be considered that its persistence provides evidence for some unknown benefit to the affected host.

Animals↗
PubMed1999

Evolutionary history of MHC class I genes in the mammalian order Perissodactyla.

We carried out an analysis of partial sequences from expressed major histocompatibility complex (MHC) class I genes isolated from a range of equid species and more distantly related members of the mammalian order Perissodactyla. Phylogenetic analysis revealed a minimum of six groups, five of which contained genes and alleles that are found in equid species and one group specific to the rhinoceros. Four of the groups contained only one, or very few sequences, indicating the presence of relatively nonpolymorphic loci, while another group contained the majority of the equid sequences identified. These data suggest that a diversification of MHC genes took place after the split between the Equidae and the Rhinocerotidae yet before the speciation events within the genus Equus.

Animals↗
PubMed1991

Primary structure of pancreatic polypeptide from four species of Perissodactyla (Przewalski's horse, zebra, rhino, tapir).

Pancreatic polypeptide (PP) has been purified from extracts of the pancreas of four species of odd-toed ungulates (Perissodactyla): Przewalski's horse, mountain zebra, white rhinoceros, and mountain tapir. The amino acid sequence of Przewalski's horse pancreatic polypeptide was established as Ala-Pro-Met-Glu-Pro-Val-Tyr-Pro-Gly-Asp10-Asn- Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr20-Ala-Ala-Glu-Leu-Arg-Arg-Tyr- Ile-Asn-Met30 - Leu-Thr-Arg-Pro-Arg-Tyr.NH2. Zebra PP was identical to Przewalski's horse PP, rhinoceros PP contained three substitutions relative to the horse (Ser for Ala1, Leu for Met3, and Glu for Gln16), and tapir PP contained one substitution relative to the horse (Leu for Met3). On the basis of morphological characteristics and the fossil record, the rhinocerotids are classified with the tapirids in the suborder Ceratomorpha, whereas the horse and zebra belong to a separate suborder, Hippomorpha. On the basis of structural similarity of the PP molecules, however, it would appear that the tapir is more closely related to the horse than to the rhinoceros. These observations provide a further example of the need for extreme caution when inferring taxonomic or phylogenetic relationships between species from the structures of homologous peptides.

Amino Acid Sequence↗
PubMed1977

[Quantitative characteristics of the systems of truncal auditory and visual brain formations in Artiodactyla and perissodactyla].

On the ground of cytoarchitectonic investigation and planimetric measurements a volumetric comparison between the systems of truncal formations of auditory and optical analysers were made in the representatives of artiodactyla (deer, elk, gazelle, sheep, wild boar, hippopotamus) and perissodactyla orders (horse). The data obtained demonstrated a great quantitative predominance of the system of optical formation in comparison with that of auditory, which correlates to the leading role of the optical system in these animals. In non-ruminants, according to other environmental conditions, vision looses its biological importance, such as in ruminants. In the former, therefore, a much less predominance of the optical formations comparing with the auditory ones was revealed. Comparisons with the previous results of the author obtained in other mammal orders, demonstrated quantative changebility--plasticity of corresponding truncal auditory, optical and vesitbular formations in response to ecologically stipulated changes of leading afferentation in different mammals.

Animals↗
PubMed1997

The caroticobasilar artery in species of order Perissodactyla.

The caroticobasilar artery was investigated in animals of order Perissodactyla, in species of Equidae family, and in lowland tapir of Tapridae family. It was found that the caroticobasilar artery forms homolateral or bilateral anastomosis between the basilar and internal carotid arteries or in horse and other species of Equidae family between basilar and caudal intercarotid arteries. The caroticobasilar artery was found in all species of Equidae family, in all zebras and in one tapir.

Animals↗
PubMed2001

Phylogenetic relationships of the five extant Rhinoceros species (Rhinocerotidae, Perissodactyla) based on mitochondrial cytochrome b and 12S rRNA genes.

A major question in rhinocerotid phylogenetics concerns the position of the Sumatran rhinoceros (Dicerorhinus sumatrensis) with regard to the other extant Asian (Rhinoceros unicornis and R. sondaicus) and African (Diceros bicornis and Ceratotherium simum) species. We have examined this particular question through the phylogenetic analysis of the complete sequences of the mitochondrial 12S rRNA and cytochrome b genes. Three additional perissodactyls (one tapir and two equids) plus several outgroup cetartiodactyls were included in the analysis. The analysis identified a basal rhinocerotid divergence between the African and the Asian species, with the Sumatran rhinoceros forming the sister group of the genus Rhinoceros. We estimate the Asian and African lineages to have diverged at about 26 million years before present.

Animals↗
PubMed1988

Interspecies variation in milk composition among horses, zebras and asses (Perissodactyla: Equidae).

Milk samples of four species of wild equids (onager, Equus hemionus onager; mountain zebra, E. zebra hartmannae; plains zebra, E. burchelli; Przewalski horse, E. caballus przewalskii) and two domesticated equids (ass, E. asinus; pony, E. caballus) were analysed. At mid to late lactation the milks of all species were very similar, containing on average 10-12% total solids, 1-2% fat, 1.6-1.8% true protein, 6-7% 'lactose', 0.3-0.5% ash, 0.08-0.12% calcium, 0.04-0.07% phosphorus and a calculated energy content of 2.0-2.4 kJ/g. Milk samples collected in the first 2 weeks after birth showed elevated levels of total solids and protein, and some had reduced 'lactose' levels, but there were no observable trends in milk composition during mid to late lactation (1-12 months post partum). It was concluded that these closely related species produce milks that are nearly identical in gross composition and that the domestic horse is a representative model for the study of equid lactation.

Animals↗
PubMed2000

Comparative cytogenetics of tapirs, genus tapirus (Perissodactyla, tapiridae).

Chromosomes of the four species of Tapirus were 2n = 52 in T. indicus, 2n = 76 in T. pinchaque, 2n = 80 in T. bairdii, and 2n = 80 in T. terrestris. The number of autosomal arms was 80-94. G-banded karyotypes indicated that a heterochromatic addition/deletion distinguished chromosomes 2 and 3 of T. bairdii and T. pinchaque, respectively. There were at least 13 conserved autosomes between the karyotypes of T. bairdii and T. terrestris, and at least 15 were conserved between T. bairdii and T. pinchaque. In G- and C-banded preparations, the X chromosomes of T. bairdii, T. indicus, and T. terrestris were identical, whereas the X chromosome of T. pinchaque differed from the X of the other species by a heterochromatic addition/deletion. The Y chromosome was a medium-sized to small acrocentric in T. bairdii, T. indicus, and T. pinchaque, but it was not positively identified in T. terrestris. There appeared to be fewer homologies between T. indicus and the three species occurring in Central and South America. Future cytogenetic studies of tapirs from the entire range of each of the four species might provide additional insight into their evolutionary biology and aid wildlife conservation efforts aimed at these threatened mammals.

Animals↗
PubMed2003

Cross-species chromosome painting in the Perissodactyla: delimitation of homologous regions in Burchell's zebra (Equus Burchellii) and the white (Ceratotherium Simum) and black rhinoceros (Diceros Bicornis).

Conserved chromosomal segments in the black rhinoceros, Diceros Bicornis (DBI, 2n = 84), and its African sister-species the white rhinoceros, Ceratotherium Simum (CSI, 2n = 82), were detected using Burchell's zebra (Equus Burchellii, EBU, 2n = 44) chromosome-specific painting probes supplemented by a subset of those developed for the horse (Equus Caballus, ECA, 2n = 64). In total 41 and 42 conserved autosomal segments were identified in C. Simum and D. Bicornis respectively. Only 21 rearrangements (20 fissions and 1 fusion) are necessary to convert the Burchell's zebra karyotype into that of the white rhinoceros. One fission distinguishes the D. Bicornis and C. Simum karyotypes which, excluding heterochromatic differences, are identical in all respects at this level of resolution. Most Burchell's zebra chromosomes correspond to two rhinoceros chromosomes although in four instances (EBU18, 19, 20 and 21) whole chromosome synteny has been retained among these species. In contrast, one rhinoceros chromosome (DBI1, CSI1) comprises two separate Burchell's zebra chromosomes (EBU11 and EBU17). In spite of the high diploid numbers of the two rhinoceros species their karyotypes are surprisingly conserved offering a glimpse of the putative ancestral perissodactyl condition and a broader understanding of genome organization in mammals.

Animals↗
PubMed1987

Molecular basis for ATP/2,3-bisphosphoglycerate control switch-over (poikilotherm/homeotherm) an intermediate amino-acid sequence in the hemoglobin of the great Indian rhinoceros (Rhinoceros unicornis, Perissodactyla).

The complete primary structure of the two hemoglobin components of the Great Indian Rhinoceros (Rhinoceros unicornis) is presented. The ratio for the two components B(alpha 2 beta I2): A(alpha 2 beta II2) is 6:4. Polypeptide subunits were separated by chromatography on CM-cellulose in a buffer containing 8M urea. The sequence was studied by degradation of the tryptic and hydrolytic cleavage products in a liquid phase sequencer. At position beta NA2 component B has Asp, whereas component A has Glu, an ATP-binding site in fish and reptilian hemoglobins. The other phosphate binding sites i.e. beta NA1 Val, beta EF6 Lys and beta H21 His are identical with 2,3-bisphosphoglycerate-(DPG)binding sites in mammalian hemoglobins, whereby rhinoceros hemoglobin resembles both ATP-sensitive poikilotherm hemoglobin and DPG-sensitive mammalian hemoglobin. The two components (beta I/beta II) additionally differ by exchange of Glu----Gly at position beta A3 and Gln----Lys at position beta GH3. The significance of these changes is discussed. Oxygenation properties of the two hemoglobins components and their dependence on ATP and DPG are given. The structure and function of Rhinoceros hemoglobin may give an insight into the evolution of the organic phosphate binding in vertebrate hemoglobins.

2,3-Diphosphoglycerate↗