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PubMed1988

Onchocerca armillata Railliet and Henry, 1909 and Onchocerca gutturosa (Neumann, 1910) in camels (Camelus dromedarius L.) in the Sudan.

A study undertaken to determine the Onchocerca species infecting camels that live in the same localities as cattle in the Dinder Region, Blue Nile Province, Sudan revealed concurrent infections with the bovine parasites Onchocerca armillata in the thoracic aorta, brachiocephalic trunks and brachial arteries and Onchocerca gutturosa in the ventral side of the lamellar parts of the ligamentum nuchae. The microfilariae of both species had the same predilection sites in the skin of the ears, head and neck regions. Those of O. gutturosa outnumber those of O. armillata but both are smaller than the respective uterine microfilariae. Males and microfilariae of both species are smaller than those of cattle origin.

Animals↗

PubMed1984

A small camel-milk protein rich in cysteine/half-cystine.

A small protein (Mr about 14 000) rich in cysteine/half-cystine has been isolated from camel milk by exclusion chromatography and reverse-phase high-performance liquid chromatography. The N-terminal amino acid sequence shows a region with several positional identities with alpha and beta-caseins, which however lack cysteine residues; positions 16-20 are identical and involve the serine residues that have been found to be phosphorylated in beta-caseins.

Amino Acid Sequence↗

PubMed1990

Scototaxis and target perception in the camel tick Hyalomma dromedarii.

The camel tick, Hyalomma dromedarii, exhibited positive scototaxis in an arena, e.g. it oriented towards a black or grey target in front of a white background. The degree of the scototactic response varied with the size and the elevation of the target, with its luminance contrast, with its shape and with the speed by which the target was moved: (1) the response to stationary and moving targets increased with increasing target size; (2) presentation of the targets at an elevation of 11 degrees--15 degrees induced the highest response; (3) the response decreased with decreasing luminance contrast of the target; (4) targets with the shape of a disk, a triangle standing on a vertex, a vertical bar or a silhouette of a dromedary caused high responses; a low response was observed when the target was a horizontal bar and there was no response to a striped pattern; (5) the smaller the size of a disk, the faster it had to be moved to elicit an optimum response. The smallest disk which elicited a significant response appeared under a visual angle of 4.8 degrees for a thick at the starting point. The smallest dromedary-shaped silhouette which elicited a significant response corresponded to the silhouette of a real dromedary at a distance of 18 m.

Animals↗

PubMed1993

Prevalence of camel brucellosis in Libya.

Sera of 967 camels of both sexes were tested for antibodies to Brucella using the Rose Bengal plate test, serum agglutination test and the complement fixation test. The prevalence of positive sera was 4.1 per cent. Samples collected for cultural examination revealed 9 isolates. Five isolates were from milk samples, 3 from aborted foetuses and one from a vaginal swab. All isolates were identified and biotyped as Brucella melitensis biovar 1.

Agglutination Tests↗

PubMed1983

Camel production in Kenya and its constraints. II. Tick infestation.

The tick loads and tick species infesting an experimental herd, a Rendille pastoralists' herd and two ranch herds of camels, in four different areas of Kenya are described. The tick species most commonly observed were Hyalomma rufipes, Hyalomma dromedarii and Rhipicephalus pulchellus.

Animals↗

PubMed1984

Brucella antibodies in Sudanese camels.

Sera of 740 camels of both sexes from three regions of Sudan were tested for antibodies to Brucella abortus. The overall incidence of antibodies was 4.9%. The highest positive number of samples (7.5%) was from the Eastern Region followed by Darfur Region (3.1%) and the Central Region (2.0%). Brucella antibodies were as frequent in males (5.6%) as females (4.5%).

Animals↗

PubMed2006

Adenosine deaminase from camel tick Hyalomma dromedarii: purification and characterization.

Adenosine deaminase is involved in purine metabolism and is a key enzyme for the control of the cellular levels of adenosine. Adenosine deaminase activity showed significant changes during embryogenesis of the camel tick Hyalomma dromedarii. From the elution profile of chromatography on DEAE-sepharose, three forms of enzyme (ADAI, ADAII and ADAIII) were separated. ADAII was purified to homogeneity after chromatography on Sephacryl S-200. The molecular mass of adenosine deaminase ADAII was 42 kDa for the native enzyme and represented a monomer of 42 kDa by SDS-PAGE. The enzyme had a pH optimum at 7.5 and temperature optimum at 40 degrees C with heat stability up to 40 degrees C. ADAII had a K (m) of 0.5 mM adenosine with higher affinity toward deoxyadenosine and adenosine than other purines. Ni(2+), Ba(2+), Zn(2+), Li(2+), Hg(2+) and Mg(2+) partially inhibited the ADAII. Mg(2+) was the strongest inhibitor by 91% of the enzyme's activity.

Adenosine Deaminase↗

PubMed2006

Camel tuberculosis--a case report.

An adult male dromedary bull was diagnosed with pulmonary tuberculosis (Tb). The dromedary was severely emaciated and died 2 months after the onset of the disease. It exhibited typical Tb lesions in both lungs and lung lymph nodes. A guinea pig inoculated with lung tissue from theTb camel died after 3 weeks from typical Tb. Mycobacteria were isolated from the dromedary's lung and lung lymph nodes and also from different organs of the guinea pig. The microorganism was identified as member of the antelope clade of the Mycobacterium tuberculosis complex.

Animals↗

PubMedDate not supplied

An abattoir survey of female genital disorders of imported camels (Camelus dromedarius) in Kano, Nigeria.

An abattoir survey of 850 female genital organs of imported camels was conducted at the Kano abattoir between October 1987 and April 1988. An incidence of 4.49% of disorders was recorded, including follicular cystic degeneration (0.12%), ovarian haemorrhagic cysts (0.47%), pyometra (0.35%), early embryonic mortality (0.12%), endometrial haemorrhages (0.47%), fetal maceration (0.12%), abscess (0.24%), vulvar tick infestation (1.77%) and cervical hypoplasia (0.12%).

Abattoirs↗

PubMed1987

Characterization of a heterogeneous camel milk whey non-casein protein.

A milk protein, occurring in the whey fraction, has been characterized from camel milk. Determination of the primary structure reveals the existence of two related types of chain with residue differences in at least the N-terminal region. A fragment representing an N-terminal part of the protein was also recovered (heterogeneous at the same positions). The absence of cysteine residues in the protein shows that no disulphide bridges are present. The pattern of fragments and a parent protein resembles that for casein and its fragments, showing that fragments and a multiplicity of forms may be typical for different milk proteins.

Amino Acid Sequence↗

PubMed1983

Testicular steroidogenesis in the camel (Camelus dromedarius) during the mating and the nonmating seasons.

Enzyme reactions in the camel testis involved in androgen synthesis were studied to determine the factors which account for the low testosterone production during the non-mating season (NMS). Testes excised during the NMS were found to have a relatively high activity of the 3 beta-hydroxysteroid dehydrogenase systems of pregnenolone, 17 alpha-hydroxypregnenolone, and dehydroepiandrosterone, but the 4-ene-17 alpha-hydroxylase and 4-ene-17,20-lyase systems were apparently less active than the 5-ene-17 alpha-hydroxylase and 5-ene-17,20-lyase. On the other hand, testes excised during the mating season (MS) were found to have a relatively high activity of 4-ene-17 alpha-hydroxylase, 4-ene-lyase, and 17 beta-hydroxysteroid oxidoreductase. The 19-hydroxylation and aromatizing activities for testosterone and androstenedione were not detected in testes excised in either season. It is proposed that during the NMS the predominant route of testosterone biosynthesis is pregnenolone leads to 17 alpha-hydroxypregnenolone leads to dehydroepiandrosterone leads to androst-5-en-3 beta, 17 beta-diol leads to testosterone.

17-alpha-Hydroxypregnenolone↗

PubMed1984

Estradiol concentration in the serum of the one-humped camel (Camelus dromedarius) during the various reproductive stages.

During the estrous cycle of the camel the concentration of estradiol (E2) varies between 9 and 110 pg/ml. In early estrus, the peak level of E2 (74.7 +/- 6.61 pg/ml, n = 11) is maintained for 2.9 +/- 1.83 days. The length of an estrous cycle is 17.2 days. In the 10th month of pregnancy the level of E2 rises abruptly to 338.3 +/- 162.42 pg/ml and continues to rise until the 12th month, peaking at 606 +/- 120.27 pg/ml. The hormone concentration then drops until the day of parturition (mean 113.4 +/- 26.51 pg/ml). The level of E2 during the nonbreeding season (May-November) is low (6-48 pg/ml).

Animals↗

PubMed1985

Evidence for somatostatin-like immunoreactivity in discrete cells of the anterior pituitary of camel (Camelus dromedarius).

Immunocytochemical methods were applied to camel pituitaries. ACTH, beta-lipotropin (LPH), LH beta, GH, TSH, and PRL immunoreactive cells were identified. They were located on different parts of anterior pituitary and had different organization and shape. In addition, somatostatin-like immunoreactivity was seen in cells situated at the top of pituitary cleft specially in a cone-shaped extension of the intermediate lobe. The role and the eventual origin of these cells have yet to be established and their occurrence related to age and life conditions.

Animals↗

PubMed1991

Activity of some enzymes in the serum of dromedary camels.

The activities of aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), acid phosphatase (ACP), lactate dehydrogenase (LDH) and isocitric dehydrogenase (ICD) in the serum of 60 healthy dromedary camels of either sex and different ages (one to 25 years) were determined. The results were analysed with respect to time of year (December-January and May-June), sex and age groups (below four years; four to 10 years; and over 10 years). The overall mean activities of AST, ALT, ALP, ACP, LDH and ICD were 36.1 +/- 0.35, 4.65 +/- 0.35, 27.21 +/- 0.43, 7.18 +/- 0.21, 479.0 +/- 7.33 and 7.74 +/- 0.17 iu litre-1, respectively. Activities of AST, ALT, ALP and ACP were significantly higher during extremely hot conditions (May-June) than in extreme cold (December-January) while the activity of LDH was higher in extremely cold conditions. Analysis of data based on sex revealed that AST, ALT and ALP activities in the serum of male animals were significantly higher than in female animals. The activities of all the enzymes were highest in animals under four years and then gradually decreased with age being lowest in the animals over 10 years.

Animals↗

PubMed1989

Brain cooling and respiratory heat exchange in camels during rest and exercise.

Respiration in relation to brain temperature (Tb) and body temperature (Tc) were investigated in two camels at rest and one during exercise (running at 10 km/h). The animals were subjected to natural ambient conditions (day: 25-30 degrees C, relative humidity (RH) about 65%; night: 15-20 degrees C, RH approx. 90%). They were studied when fully hydrated and during progressive dehydration by up to 15% of initial weight. At low Tc (less than 38 degrees C) Tb greater than Tc by approximately 0.2 degrees C, at higher Tc significant brain cooling was observed by as much as 1.5 degrees C during exercise. Minute ventilation (VE) and respiratory rate (f) increased with Tc such that tidal volume was constant and similar at rest and during exercise (Tc-Tb) increased linearly with f and hence VE. The cooling, dependent on turbinate heat exchange was related to certain features of the air flow pattern and f which have also been described in other large mammals.

Animals↗

PubMed1995

Monoclonal antibodies against camel (Camelus dromedarius) IgG, IgM and light chains.

Monoclonal antibodies specific for camel IgG and IgM heavy chains and immunoglobulin light chains were produced by a simple, time-saving and efficient method. Popliteal lymph nodes isolated 9 days after a primary foot-pad immunisation were used as the source of antibody producing hybridoma cells. Ascites was induced in mice and ascitic fluid collected. The specificity of anti-IgG and anti-IgM monoclonal antibodies was determined by enzyme-linked immunosorbent assay (ELISA) and Western blotting. Monoclonal antibodies specifically reacting to IgG1 subclasses were demonstrated; no monoclonal antibodies specific to IgG2 or IgG3 were generated. An unexpected finding was that some class-specific monoclonal antibodies were light chain, and not heavy chain, reactive.

Animals↗

PubMed1986

Characterization of a camel milk protein rich in proline identifies a new beta-casein fragment.

A camel milk whey protein has been isolated by reverse-phase high performance liquid chromatography. The protein is, like caseins, rich in proline (25% of the whole protein). The N-terminal amino acid sequence shows that the protein is homologous with a C-terminal region of beta-caseins analyzed from other species. The protein is concluded to be a fragment of beta-casein, derived from a non-tryptic type of cleavage of the parent molecule, and increasing the multiplicity of known casein products.

Amino Acid Sequence↗

PubMed1996

Kinetic properties of purified carnitine acetyltransferase from the skeletal muscle of Arabian camel (Camelus dromedarius).

The kinetic properties of carnitine acetyltransferase from the skeletal muscle of the Arabian camel (Camelus dromedarius) were studied. The enzyme showed an optimum pH between 7.2 and 8.2. Reciprocal plots of data obtained by varying one substrate concentration while keeping the other constant revealed lines that converged on the abscissa, indicating that the enzyme possible follows a random mechanism of catalysis. The Kms for L-carnitine and acetyl-coenzyme A were 244 and 44 microM respectively, while those for acetyl-DL-carnitine and coenzyme A (Co A) were 307 and 39 microM respectively. The Km for one substrate was found to be independent of the concentration of the second substrate used. Corresponding Vmax values for L-CA, acetyl-Co A, acetyl-DL-carnitine and Co A are 98, 98, 102 and 100 mumol min-1 mg-1 protein respectively. The low Km obtained for acetyl-DL-carnitine suggests an adaptive mechanism in this desert species for enduring prolonged dry spells without food and water.

Acetyl Coenzyme A↗