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At least 37 records · Page 2Linked to original sources
PubMed1999

The caudal intercarotid artery in species of order perissodactyla.

The caudal intercarotid artery was investigated in 6 species of Equidae family and in lowland tapir of Tapiridae family. It was found that this artery connects bilateral intracranial segments of the internal carotid artery. It is located in the cavernous and intercavernous sinuses, caudal to the hypophysis. This artery being constant vessel in horse, is also permanent vessel in other species of Equidae family. It is homologous with anastomising vessel in fishes, amphibia, reptiles and birds.

Animals↗
PubMed2005

Comparative morphological study on the tongue and lingual papillae of horses (Perissodactyla) and selected ruminantia (Artiodactyla).

A common characteristic of horses, Rocky Mountain goats, and cattle is that they all have a well developed lingual prominence on the dorsal surface of the posterior area of the tongue. Foliate papillae were found in the horse studied but not in the goat or in cattle. The horse filiform papillae had a long and slender external form with a thin and slender CTC, while in the goat and cattle the external form consisted of a large thick main process and the CTC consisted of a bundle of numerous rod-shaped protrusions. The special papilla found on the lingual prominence resembled larger filiform-like papillae in the horses; however, in the goat and cattle it was a very thick and large tongue like papillae. The horses had two large vallate papillae, while the goat and cattle had 15 or more vallate papillae at the posterior area of the lingual prominence. This suggests that the fine structure of horse tongues may display a more primitive pattern than that present in goats and cattle.

Animals↗
PubMed1984

[Perissodactyla: the primary structure of hemoglobins from the lowland tapir (Tapirus terrestris): glutamic acid in position 2 of the beta chains].

The hemoglobins from a lowland tapir (Tapirus terrestris) were analysed and the complete primary structure is described. The globin chains were separated on CM cellulose column in 8M urea and the amino-acid sequences were determined in the liquid phase sequenator. The results show that globin consists of two alpha chains (alpha I and alpha II) and beta major and beta minor components. The alpha chains differ only at one position: alpha I contains aspartic acid and alpha II glycine. The beta chains are heterogeneous: aspartic and glutamic acid were found at position beta 21 and beta 73 of the beta major components and asparagine and serine at position beta 139. In the beta minor components four positions were found with more than one amino acid, namely beta 2, beta 4, beta 6 and beta 56. The sequences are compared with those of man, horse and rhinoceros. Four residues of horse methemoglobin, which are involved in the alpha 1 beta 1 contacts are substituted in tapir hemoglobins. In the alpha chains: alpha 107(G14)Ser----Val, alpha 111-(G18) Val----Leu, alpha 115(GH3) Asn----Asp or Gly; in the beta chains: beta 116(G18) Arg----Gln. The amino acid at beta 2 of the major components is glutamic acid while glutamine and histidine are found in the minor components. Although glutamic acid, a binding site for ATP, does not interact with 2,3-bisphosphoglycerate, glutamine and histidine in the minor components are responsible for the slight effect of 2,3-bisphosphoglycerate on tapir hemoglobin.

Amino Acid Sequence↗
PubMed1998

Chromosomal rearrangements in a Somali wild ass pedigree, Equus africanus somaliensis (Perissodactyla, Equidae).

Chromosome analyses were conducted on 15 animals in a pedigree of Somali wild ass, Equus africanus somaliensis. G- and C-banded karyotypes are presented for the first time on this endangered species. The diploid number ranged from 62 to 64. Numerical chromosomal variation was the result of a centric fission which was accompanied by a heterochromatic deletion. The fission polymorphism involved acrocentric elements 19 and 21 as determined by G-banding. These autosomes are homologous to those involved in centric fission/fusion polymorphisms in other equids: E. asinus (domestic donkey), E. hemionus (onager), E. kiang (kiang), and E. burchelli (common zebra). Banding analyses also revealed a paracentric inversion polymorphism in submetacentric chromosome pair 2 of E. a. somaliensis. Both the centric fission and paracentric inversion polymorphisms involved heterochromatic regions. One individual was found to be heterozygous for two de novo chromosomal rearrangements: a centric fission (involving acrocentric elements 19 and 21) and a heterochromatic deletion of chromosome 2.

Animals↗
PubMed1984

The primary structure of monomeric beta-lactoglobulin I from horse colostrum (Equus caballus, Perissodactyla).

beta-Lactoglobulin-like proteins were detected in horse colostrum and normal milk using immunological techniques. In contrast to the beta-lactoglobulins sequenced so far these proteins are monomeric and genetically not homogenous. In this paper we report the first primary structure of a monomeric beta-lactoglobulin from horse colostrum. By means of an automatic liquid-phase sequenator the sequence of peptides obtained by tryptic digestion and by cyanogen bromide cleavage was determined. A limited tryptic digestion and hydrolysis with chymotrypsin provided the necessary overlapping peptides. The horse beta-lactoglobulin I consists of 162 amino acids, among these four cysteine, six methionine residues and one tryptophan residue. Homologous comparison with bovine beta-lactoglobulin A shows an unexpectedly great difference of 72 amino acids (or 44%). Thirteen of these exchanges are explained as two-point mutations. We found that the free thiol group, localized at position 121 or in equal amounts at positions 119 and 121 in bovine beta-lactoglobulin, is absent in beta-lactoglobulin I from horse colostrum. In position 121 a tyrosine substitution for cysteine was found. The amino-acid exchanges of the horse beta-lactoglobulin I as compared to the other beta-lactoglobulins are discussed.

Amino Acid Sequence↗
PubMed1985

The amino-acid sequence of beta-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): beta-lactoglobulins are retinol-binding proteins.

beta-Lactoglobulin isolated from horse colostrum is heterogeneous and contains two components: beta-lactoglobulin I and beta-lactoglobulin II. These two proteins are monomeric and show differences in their electrophoretic mobilities, chain lengths and primary structures. The complete amino-acid sequence of beta-lactoglobulin II was determined by automated Edman degradation of the intact protein and of the peptides derived from these by digestion with trypsin or chymotrypsin and by chemical cleavage with cyanogen bromide. Unlike other beta-lactoglobulins which contain 162 amino acids, horse beta-lactoglobulin II is unique in that it contains 166 amino acids. The additional four amino acids represent an insertion between positions 116 and 117 of other beta-lactoglobulins so far sequenced, including horse beta-lactoglobulin I. Sequence comparison of beta-lactoglobulins I and II from horse colostrum reveals 48 amino acid substitutions (30%). Such a diversity between members of the beta-lactoglobulin gene family has not been encountered before. Sequence comparison with bovine beta-lactoglobulin A shows 85 amino acid replacements accounting for 53% of the residues. The structural homology with human retinol-binding protein may reveal similar biological functions and clues to the origin of milk proteins.

Amino Acid Sequence↗