Studies on avian erythrocyte metabolism. Inositol tetrakisphosphate: the major phosphate compound in the erythrocytes of the ostrich (Struthio camelus camelus).
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Mating-induced luteinizing hormone surge and ovulation in the female camel (Camelus dromedarius).
Blood samples were collected after mating from four female one-humped camels every 10 min for 9-12 h. Luteinizing hormone (LH) was quantified in plasma by radioimmunoassay using antibovine LH. Of the seven observed matings, five were followed by a release of LH, and three by an ovulation (indicated by a subsequent secretion of progesterone). LH levels at the time of mating ranged from 0.7 to 3 ng/ml. When an LH response occurred, the levels increased 1 h after mating and reached a maximum in 2-3 h (ranging from 2.9 to 19.1 ng/ml). A decrease in LH was observed starting 6 h after mating and lasting for 6 h. These results are in agreement with a coitus-induced mechanism of ovulation in the one-humped camel (Camelus dromedarius). They confirm and extend the observations reported in the bactrian camel (Camelus bactrianus).
Animals↗
Ultrastructure of the nephron of the one-humped camel, Camelus dromedarius.
The nephron of the one-humped camel Camelus dromedarius was investigated by light and transmission electron microscopy. Besides the many features common to other mammalian kidneys, the nephron of the camel is unique in having an unusually thick basal lamina underlying the epithelial cells of the nephron, the thickest being found in part of the parietal layer of Bowman's capsule and the thin limb of the loop of Henle. In the latter, the membrane usually appears lamellated and contains numerous tiny vesicles. In other parts of the nephron, the basal lamina usually has a homogenous appearance. The possible significance of the thickening of the basal lamina is discussed in relation to the general high renal efficiency of the camel.
Animals↗
A survey on spontaneous atherosclerosis of camels (Camelus dromedarius) in Iran.
In a survey carried out on 200 camels (Camelus dromedarius) from different parts of Iran, three cases were diagnosed positive for atherosclerosis on gross and microscopic examination. A sex and age predilection is suspected. The complications of atherosclerosis were not present. To the best of the authors' knowledge this is the first report of atherosclerosis in camels.
Age Factors↗
zeta-Crystallin is a major protein in the lens of Camelus dromedarius.
Camel (Camelus dromedarius) lenses contain a protein with an apparent subunit Mr 38,000 that constitutes approximately 8-13% of the total protein. The protein has been purified and has a native Mr 140,000 as determined by gel filtration. This is consistent with its being a tetramer. The protein reacts with antibodies raised against both guinea pig zeta-crystallin and peptides corresponding to amino acids 1-10 and 295-308, but not to antibodies raised against amino acids 320-328 of zeta-crystallin. Based on these criteria it is concluded that this protein, which is a major constituent of camel lens, is zeta-crystallin. This may be the first example of a protein (enzyme) being independently utilized as a crystallin in the lens of species from two mammalian orders.
Animals↗
Studies on camel hemoglobin. 1. Physico-chemical properties and some structural aspects of camel hemoglobin (Camelus dromedarius).
Hemoglobin from an adult camel (Camelus dromedarius) was prepared from the red cell lysate by CM- and DEAE-cellulose chromatography. The purified hemoglobin showed a lesser mobility on starch gel electrophoresis at pH 8.5 than that of human hemoglobin C. Native camel hemoglobin contains 95-99% alkali-resistant hemoglobin and in soluble in 2.94 M K2HPO4/KH2PO4 buffer. Different forms of camel hemoglobin show similar ammonium sulfate precipitation curves. Indirect evidence for the stability of camel hemoglobin solutions was obtained from several sources. Spontaneous met-hemoglobin formation is extremely slow and minimal quantities of degradation products appear on starch gel electrophoresis and on chromatographic separation. The alpha and beta chains of camel hemoglobin A were separated on a CM-23 column by the use of a pyridine formate gradient. Large peptide fragments were obtained by tryptic digestion of maleylated alpha and beta chains. The N-terminal structure of the alpha and beta chains and of tryptic maleylated peptides derived from alpha and beta chains are presented. Between adult camel hemoglobin and adult human hemoglobin six amino acid differences in the N-terminal 20 amino acid residues of the alpha chain, at residues: 4, 5, 12, 14, 17, and 19; eight amino acid substitutions were found in the beta chain at positions: 4, 5, 6, 9, 12, 13, 16, and 19. Substitutions at alpha5 Ala leads to Lys, and beta19 Asn leads to Lys, increase the net positive charge of camel hemoglobin by two, while other substitutions result in no charge differences. The molecular basis of the stability of camel adult hemoglobin is discussed.
Amino Acid Sequence↗
Effect of inositol hexakisphosphate on the EPR properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin. Evidence for two polyanion binding sites.
The effect of inositol hexakisphosphate on the EPR properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin has been investigated at 110 K. In the absence of inositol hexakisphosphate, the nitrosyl derivative of dromedary hemoglobin shows an EPR spectrum with a rhombic shape and a weak hyperfine splitting in the gz region, a feature that is generally taken as characteristic of the high-affinity state of tetrameric hemoproteins. On addition of 1 mole of inositol hexakisphosphate/tetramer, three new hyperfine lines (Az = 1.7 mT), centered at gz = 2.01, appear; this type of spectrum is indicative of the low-affinity state of hemoglobins. A further addition of inositol hexakisphosphate, corresponding to a 20-fold molar excess, completely reverses the polyphosphate-dependent transition, giving an EPR spectrum that is exactly superimposable to that observed in the absence of the allosteric effector, i.e., is typical of the high-affinity state of the macromolecule. Both in the absence and presence of inositol hexakisphosphate, the EPR spectra are virtually independent of pH in the range explored (from 5.5 to 7.5). These results, taken together with the behavior of the nitric oxide derivative of human hemoglobin, provide further evidence for the existance in dromedary hemoglobin of two polyanion binding sites that affect in an opposite way the conformational equilibrium of the macromolecule.
Animals↗
Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin.
The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopic (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.
2,3-Diphosphoglycerate↗
Binding of inositol hexakisphosphate to the oxygenated derivative of dromedary (Camelus dromedarius) and human hemoglobin: 31P-NMR study.
Binding of inositol hexakisphosphate (IHP) to the oxygenated derivative of dromedary (Camelus dromedarius) and human hemoglobin (Hb) was investigated by 31P-NMR. The results obtained show that dromedary Hb binds, with different affinity, two IHP molecules per tetramer at distinct sites, while human Hb binds only one IHP molecule per tetramer.
Animals↗
Determination of the primary and secondary structures of the dromedary (Camelus dromedarius) prolactin and comparison with prolactins from other species.
A non-glycosylated form of camel prolactin (camPRL), isolated from one-humped camel (Camelus dromedarius) pituitaries, was totally sequenced. A glycosylated form, separated by affinity chromatography on ConA-Sepharose, was partially sequenced. The comparison of the N-terminal amino acid sequences of the glycosylated and non-glycosylated forms showed that the only putative site of N-glycosylation (Asn-31) was indeed glycosylated. The far ultraviolet (UV) circular dichroism (CD) spectra of the two isohormones were identical, suggesting that the carbohydrate moiety had no effect on the global camPRL secondary structure. The far UV circular dichroism spectra of the two isohormones were analyzed in order to determine their relative proportions of periodic secondary structure, 60% of which was found to be in alpha-helix, as in prolactins of other species. The dromedary sequence was compared to those of other species and interpreted in term of evolutionary process. As already found for gonadotropins, the closest species to the dromedary was found to be the pig.
Amino Acid Sequence↗
The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine.
1. The disaccharidases, cellobiase, isomaltase, lactase, maltase, sucrase and trehalase were investigated for presence in the camel (Camelus dromedarius) intestine and pancreas. All, except sucrase, were present. 2. Their levels of activities were measured at different positions of the small and large intestines and the location of maximum level of activity for each enzymes along the intestinal tract was established. 3. High levels of activities were determined in the contents of the intestinal lumen and, therefore, it is absorbed into the cells of the epithelial villi and hydrolyzed there. 4. The possibility of carbohydrate digestion in camel intestine is discussed.
Animals↗
Selective brain cooling in desert animals: the camel (Camelus dromedarius).
1. Animals living in the Arabian desert are subjected to extremely high temperatures during the day in summer and very cold nights in winter. They have developed various adaptive mechanisms in order to cope with these severe heat conditions. 2. The camel (Camelus dromedarius), like many other land animals, resorts to selective brain cooling when it is subjected to heat stress. 3. This mechanism protects the heat-sensitive brain tissue from heat stress and at the same time increases the animals' tolerance to high temperatures. 4. The blood cooled in the nasal cavity by evaporative heat loss is diverted to the brain sinuses via the nasal and angular veins. 5. In the cavernous sinus, the arterial blood in the carotid rete is cooled by the cold venous blood before entering the brain. This will lead to significant cooling of the brain tissue. 6. Active myogenic tone was mainly observed in the facial, nasal and angular oculi veins of the camels head. This tone was found to be sensitive to small changes in temperature in the range 33-45 degrees C. 7. The facial veins constricted, while the nasal and angular oculi veins relaxed to increasing temperatures. This leads to a coursing of cold venous return to the brain's sinuses for selective brain cooling. 8. It is concluded that this myogenic vasoactive mechanism is a major factor in the control of blood flow in the facial area of the camel during heat stress.
Animals↗
Camel (Camelus dromedarius) and sheep (Ovis aries) meat as a source of dog infection with some coccidian parasites.
Experimental infection of dogs with camel (Camelus dromedarius) meat resulted in infection of the dogs with Isospora canis, Hammondia heydorni and Sarcocystis cameli. The dogs fed sheep (Ovis aries) meat passed oocysts of Isospora canis, Isospora ohioensis and sporocyts of Sarcocystis spp. Extraintestinal stages were detected in the intestinal lymph node of a rabbit killed 4 days following inoculation with Isospora ohioensis oocysts. Dogs fed the rabbit (killed 4 days after inoculation with I. ohioensis) passed I. ohioensis oocysts in their faeces 8 days post-infection.
Animals↗
Lens aldo-keto reductase of Camelus dromedarius: purification and properties.
Aldo-keto reductase has been purified 13,000-fold from the lens of the camel (Camelus dromedarius) to a specific activity of 85 U/mg protein. The enzyme is a monomeric protein, exhibiting a Mr = 40,000 upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. Camel lens aldo-keto reductase shows a broad substrate specificity, which is strictly dependent on NADPH, and is insensitive to inhibition by Sorbinil and valproate. Aldoses with a carbon chain with more than four residues, as well as glucuronate, are not reduced by the enzyme. On the basis of substrate specificity and sensitivity to inhibition, camel lens aldo-keto reductase appears to be distinct from the so far described aldose, aldehyde and carbonyl reductases.
Alcohol Oxidoreductases↗
Fatty acid composition of hump triglycerides of the camel Camelus dromedarius.
1. Hump lipids of Camelus dromedarius (single-humped camel) were extracted and fractionated by thin-layer chromatography. 2. The hump lipids were found to be mainly triglycerides with a trace of phospholipids. 3. The fatty acid methyl esters of the triglycerides were studied by gas-liquid chromatography. 4. The major fatty acids were found to be palmitate (35%), stearate (26%), oleate (24%) and myristate (12%). Hexadecenoic (2%) and pentadecanoic acids were minor components.
Adipose Tissue↗
A comparative study of ketone body metabolism between the camel (Camelus dromedarius) and the sheep (Ovis aries).
1. Plasma levels of beta-hydroxybutyrate (BHB), and acetoacetate (AcAc) have been measured in camels (Camelus dromedarius) and sheep (Ovis aries). The activity of beta-hydroxybutyrate dehydrogenase (BHB-deH2) (E.C. 1.1.1.30) was studied in the rumen epithelium and the liver of these animals. 2. Concentrations of plasma BHB and AcAc in the camel were in respective order 33 and 4 times lower than that of the sheep. The ratios of BHB to AcAc were 0.61 and 4.8 for the camel and sheep, respectively. 3. The activity of BHB-deH2 in the rumen epithelium of the camel and sheep were 7.15 and 66 mumol/hr/g wet wt tissue, respectively. The activity in both species was higher in the rumen epithelium than in the liver.
Acetoacetates↗
Levels of glycosylated haemoglobin in the Arabian camel (Camelus dromedarius).
Proportions of glycosylated haemoglobin (Hb) were determined in 10 Arabian camels (Camelus dromedarius) and were compared with normal controls (n = 59) and diabetic patients (n = 47) using the thiobarbituric acid (TBA) method. The level of glycosylated haemoglobin (5.5%) in camels is significantly different from that of normal healthy humans (4.9%) (P less than 0.001). Whereas the glucose levels were comparable, this difference in percentages of glycosylated haemoglobin may be explained by the difference in survival time between human and camel red blood cells.
Animals↗
Liver uricase in Camelus dromedarius: purification and properties.
1. Uricase (urate: oxygen oxidoreductase, EC 1.7.3.3) was purified 750-fold from the liver of Camelus dromedarius. 2. The enzyme is a tetramer with a Mr of 100,000, displays high specificity for uric acid with a Km of 12 microM and is inhibited by a selected number of purine derivatives carrying oxygen at the C2 position. 3. The effect of pH and the inhibition by thiol compounds and chelating agents on the enzyme activity is reported. 4. Some lines of evidence suggesting the possibility of interaction of camel liver uricase with oligonucleotides are presented.
Animals↗