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At least 1,135 records · Page 63Linked to original sources
PubMed1993

Typing of artiodactyl MHC-DRB genes with the help of intronic simple repeated DNA sequences.

An efficient oligonucleotide typing method for the highly polymorphic MHC-DRB genes is described for artiodactyls like cattle, sheep and goat. By means of the polymerase chain reaction, the second exon of MHC-DRB is amplified as well as part of the adjacent intron containing a mixed simple repeat sequence. Using this primer combination we were able to amplify the MHC-DRB exons 2 and adjacent introns from all of the investigated 10 species of the family of Bovidae and giraffes. Therefore, the DRB genes of novel artiodactyl species can also be readily studied. Oligonucleotide probes specific for the polymorphisms of ungulate DRB genes are used with which sequences differing in at least one single base can be distinguished. Exonic polymorphism was found to be correlated with the allele lengths and the patterns of the repeat structures. Hence oligonucleotide probes specific for different simple repeats and polymorphic positions serve also for typing across species barriers. The strict correlation of sequence length and exonic polymorphism permits a preselection of specific oligonucleotides for hybridization. Thus more than 20 alleles can already be differentiated from each of the three species.

Alleles↗
PubMed1976

Studies on the primary structure of bison pancreatic ribonuclease.

Bison pancreatic ribonuclease was isolated by affinity chromatography. Thermolysin and tryptic digestion of denaturated protein, and subtilisin digestion of native protein yielded peptides, which were purified and submitted to amino acid analysis. These peptides, together with partial sequence data obtained by Stewart & Stevenson (16) overlap the entire amino acid sequence of bison ribonuclease. No differences with bovine ribonuclease were found, although there may be differences in state of amidation of some residues.

Amino Acid Sequence↗
PubMed1981

Isolation and characterization of alpaca growth hormone.

A simple and mild procedure is described for the isolation of pituitary growth hormone from alpaca glands. It involves extractions in buffer at pH 8.7 and gel filtration in Sephadex G-75. an average yield of 1 mg purified product may be obtained from 1 g fresh alpaca pituitary glands. The alpaca hormone was examined for homogeneity by SDS-polyacrylamide gel electrophoresis, gel electro-focusing and end-group analyses. It is a protein composed of a single polypeptide chain with phenylalanine at both ends. The C-terminal sequence is -Ala-Phe. The molecular weight is approximately 21 700 and the amino acid composition very similar to that observed in equine growth hormone.

Amino Acids↗
PubMed1976

Carbohydrate in pancreatic ribonucleases.

A survey of the presence and compositions of carbohydrate chains attached to pancreatic ribonucleases is given. Carbohydrate chains may occur at asparagine residues in Asn-X-Ser/Thr sequences at four exposed sites of the molecule (positions 21, 34, 62 and 76). These sites form part of highly variant sequences in pancreatic ribonucleases with the consequence that the enzymes from very closely related species may differ in the presence or absence of carbohydrate. In a number of ribonucleases Asn-X-Ser/Thr sequences occur which carry carbohydrate in only a part of the molecules. The occurrence of Asn-X-Ser/Thr sequences entirely without any carbohydrate also has been demonstrated. Compositions of the carbohydrate moieties of ribonucleases from cow, sheep, pig, whales, giraffe, okapi, moose, horse, coypu, chinchilla, and guinea-pig are presented. Striking differences in complexity have been found, both between chains attached to the same site in different species (cow and giraffe), between chains attached to different sites of the same enzyme in one-species (pig) and even between chains attached to the same site in a single species (chinchilla).

Animals↗
PubMed1980

Pancreatic ribonucleases of mammals with ruminant-like digestion. Amino-acid sequences of hippopotamus and sloth ribonucleases.

High levels of pancreatic ribonucleases are found in ruminants, species that have a ruminant-like digestion and several species with coecal digestion. Pancreatic ribonucleases from several independently evolved species with ruminant-like digestion were investigated to test a hypothesis that glycosylation of ribonucleases may have some function in species with coecal digestion and that glycosylation of the enzyme may not be advantageous for ruminants. Ribonucleases from the hippopotamus, two-toed sloth and three-toed sloth were isolated by extraction with sulfuric acid and affinity chromatography. Complete amino acid sequences were determined for the ribonucleases from the hippopotamus and two-toed sloth and a partial sequence for the enzyme from the three-toed sloth. The amino acids 75-78 of hippopotamus ribonuclease were positioned by homology with other artiodactyl ribonucleases. In hippopotamus ribonuclease a heterogeneity was found at position 37, half of the molecules containing glutamine acid the other half lysine. Hippopotamus ribonuclease differs less from pig and bovine ribonuclease than these differ from each other, because more ancestral characteristics have been retained. Although hippopotamus ribonuclease contains all four Asn-X-Ser/Thr sequences previously found to be glycosylation sites in one or more pancreatic ribonucleases, only the sequence Ans-Met-Thr (34-36) is glycosylated in the variant with glutamine at position 37, while the variant with lysine at this position is carbohydrate-free. Both sloth ribonucleases are completely glycosylated at the sequence Ans-Met-Thr (34-36) with a simple type of carbohydrate chain. The amino acid sequence of two-toed sloth ribonuclease shows some interesting coupled replacements.

Amino Acid Sequence↗
PubMed1985

Existence of ternary complexes of procarboxypeptidase A in the pancreas of some ruminant species.

The existence of procarboxypeptidase A, in the form of a non-covalent ternary complex containing the apparently inactive serine protease (subunit III), has so far been observed only in the ox pancreas. Evidence, obtained in the present study, shows that a ternary complex of procarboxypeptidase A, with a subunit III highly homologous with that of the bovine complex, is also present in two other ruminant species, sheep and goat. The biological significance of these complex forms of procarboxypeptidase A and the consistently high biosynthesis level of the apparently inactive subunit III in all three ruminant species is still unknown. Yet the synthesis of subunit III is not related to the animal diet since in the horse, which is a non-ruminant herbivorous animal, the procarboxypeptidase A is monomeric. Reassociation assays between either bovine subunits II or III and monomeric as well as binary forms of procarboxypeptidase A from various species show that, unlike subunit II, the recognition site for subunit III is highly conserved in all the procarboxypeptidases A and that bovine subunit II is different from porcine chymotrypsinogen C with regard to association.

Amino Acid Sequence↗
PubMed1990

Interaction of hemoglobin with chloride and 2,3-bisphosphoglycerate. A comparative approach.

The equilibrium oxygen-binding properties of hemoglobins from reindeer (Rangifer tarandus tarandus), musk ox (Ovibos muschatos) and a bat (Rousettus aegyptiacus) have been investigated with special reference to the effect of heterotrophic ligands such as chloride and 2,3-bisphosphoglycerate [Gri(2,3)P2]. The results obtained with hemoglobins from reindeer and musk ox indicate that their low oxygen affinity and their insensitivity to Gri(2,3)P2 are not only an intrinsic property of the molecule, as proposed in the case of ruminant hemoglobins, but also the results of the interplay between chloride and Gri(2,3)P2 interactions. In other words, insensitivity of reindeer and musk ox hemoglobins to Gri(2,3)P2 is mainly due to a decreased affinity constant for this cofactor and to an increased affinity constant for chloride anions; this renders more effective the competition of chloride for th anion-binding site. On the other hand bat hemoglobin behaves in a completely different way and could be regarded as a type case of low-affinity hemoglobin since its functional properties are modulated neither by chloride nor by Gri(2,3)P2. The results are discussed in the light of the amino acid residues which are known to be involved in the binding of organic phosphates.

Allosteric Regulation↗
PubMed1989

Osteomorphological features of the appendicular skeleton of gazelles, genus Gazella Blainville 1816, bohor reedbuck, Redunca redunca (Pallas, 1767) and bushbuck, Tragelaphus scriptus (Pallas, 1766).

Examined the osteomorphological features of the appendicular skeleton of Grant's gazelle (Gazella granti), bohor reedbuck (Redunca redunca) and bushbuck (Tragelaphus scriptus). Osseous remains of these medium sized antelopes are often encountered in African late Quaternary archaeological sites, but their specific identification poses considerable problems to the archaeozoologist. A key has been developed to meet this recurrent problem and a number of diagnostic osteomorphological features, allowing a distinction between the bovids mentioned, are established. The osteomorphological characteristics, typical for Grant's gazelle have also been observed in the eight other extant African gazelles and in two Asian species, the goitred gazelle (Gazella subgutterosa) and the mountain gazelle (Gazella gazella).

Animals↗
PubMed1990

Postcranial osteology of the most primitive artiodactyl Diacodexis pakistanensis (Dichobunidae).

Diacodexis pakistanensis is the smallest and most primitive artiodactyl. It is known from the early Eocene of the Indo-Pakistani subcontinent. It retains a clavicle, has five complete digits in the manus and four in the pes and is digitigrade. The elongated limbs, reduced ability to pronate and supinate, double pulleyed astragalus and reduced lateral digits indicate that D. pakistanensis is cursorial. However, the shape of the spinous processes of the sacrum, the size of the deltoid tubercle of the humerus, the shape of the proximal femur, the narrow distal trochlea of the astragalus and proportions of the long bones indicate that it is less cursorial than any other dichobunid artiodactyl.

Animals↗
PubMed1994

Renal anatomy of the pigmy hippopotamus (Choeropsis liberiensis): an overview.

The adult kidney of Choeropsis liberiensis is 74.8% cortex and 22.9% medulla. The neonatal cortex is relatively less. A single kidney has about 3 x 10(6) glomeruli. These form 5% of renal mass in the adult but more so in neonates. The primary tubus maximus, TM1, follows the lateral curvature of the kidney. It gives off, toward the hilum, dorso-ventrally paired secondary tubi maximi, TM2. The tubi are a single layer of high cuboidal epithelium from which terminal collecting ducts arise throughout the surrounding inner medulla. The cranial and caudal limbs of TM1 open at a diminutive pelvis which receives a small papilla in continuity with TM1. The medulla is continuous although variably distorted by folds of cortex at the lateral curvature of the kidney. The renal lobes project toward the medial border and consist of cortex, medulla and TM2. The lobar cortex is continuous with the common cortex of the lateral curvature. The kidney, although strongly lobed, has no infundibula or rencules. A main peripheral vein courses medial and parallel to TM1. It is apparently a modified large arcuate vein and receives arcuate and interlobar tributaries. At the level of the papilla it joins the main renal vein. The arterial supply is mainly by interlobar arteries but there are also sizeable external perforator arteries which branch from the main renal artery and perforate the cortex of lobes about the hilum. The source of the arteries is illustrated.

Animals↗