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PubMed1989

Eimeria capricornis n.sp., E. nihonis n.sp., E. naganoensis n.sp., and E. kamoshika n.sp. (Protozoa: Eimeriidae) from the Japanese serow, Capricornis crispus.

Eimeria capricornis n.sp., E. nihonis n.sp., E. naganoensis n.sp. and E. kamoshika n.sp. were detected from the Japanese serow, Capricornis crispus. The oocysts of these species were ovoid to ellipsoid, measuring 48.02 +/- 0.53 x 33.93 +/- 0.35 microns, 29.73 +/- 0.45 x 21.01 +/- 0.29 microns, 20.04 +/- 0.05 x 15.77 +/- 0.04 microns and 30.02 +/- 4.24 x 14.58 +/- 2.03 micron, respectively. In all the species the micropyle was observed, but the micropylar cap and oocyst residuum were not present. The polar granules were observed in the oocysts of E. capricornis. The sporocysts of the above species were spherical to elongate ovoid, measuring 15-23 x 8-13 microns, 14-16 x 7-10 microns, 11-13 x 6-8 microns and 8-10 x 6-7 microns, and the sporulation time was 6, 3, 3 and 6 days, respectively. The sporocyst residuum and refractile body were seen in all the species. In the sporocysts of E. naganoensis and E. kamoshika tiny Stieda body was seen, but not in the other two species. These four Eimeria species were not infective to goats.

Animals↗
PubMed1985

Primary structure of the hemoglobins from the greater Kudu antelope (Tragelaphus strepsiceros).

The adult greater Kudu antelope has two hemoglobin components, Hb A and Hb B, with one alpha and two beta chains. The complete amino-acid sequences of these three chains are presented. The two beta chains differ only in one residue at position 16 (Gly----Ser) and may be the product of two allelic genes. The primary structure of the chains was determined by sequencing the tryptic peptides after their isolation from the tryptic digest of the chains by high performance liquid chromatography. The alignment of these peptides was deduced from homology with the chains of bovine hemoglobin. Between the Kudu hemoglobins and those of cattle a high degree of homology was found.

Amino Acid Sequence↗
PubMed1986

Interaction of allosteric effectors with alpha-globin chains and high altitude respiration of mammals. The primary structure of two tylopoda hemoglobins with high oxygen affinity: vicuna (Lama vicugna) and alpaca (Lama pacos).

Polyacrylamide gel electrophoresis and ion-exchange chromatography revealed one hemoglobin component for vicuna (Lama vicugna) and alpaca (Lama pacos). Following chain separation by chromatography on carboxymethyl-cellulose, the amino-acid sequences were elucidated for the alpha- and beta-chains of both hemoglobins using automatic Edman degradation of the chains and the tryptic peptides. Vicuna and alpaca have identical beta-chains showing no substitutions to llama (Lama glama) either. In the alpha-chains alpaca differs from llama by the exchange of one amino-acid residue: alpha 122(H5)Asp----His. The same substitution is present in vicuna too, but in addition we found two more exchanges: alpha 10(A8)Ile----Val and alpha 130(H13)Ala----Thr. The close relationship between llama and alpaca suggests that they both originate from the wild guanaco, and there is no domesticated form of vicuna. The sequence data show that the higher oxygen affinity in vicuna compared to llama and alpaca must be due to the alpha-chains as the beta-chains are identical. The significance of the substitutions in alpha 122(H5), an alpha 1/beta 1-contact, and alpha 130(H13) is discussed.

Altitude↗
PubMed1986

[Primary structure of hemoglobin of the polar bear (Ursus maritimus, Carnivora) and the Asiatic black bear (Ursus tibetanus, Carnivora].

The adult Polar and Asiatic Black Bear have one hemoglobin component each. The complete amino-acid sequences of their alpha- and beta-chains are presented. Their primary structures were determined by sequencing the tryptic and prolyl peptides. The alignment of these peptides was deduced from homology to human hemoglobin chains. The hemoglobin sequences of the two species proved to be identical. The evolutionary aspects of this result are discussed. A table of identical hemoglobin sequences from different species is given.

Amino Acid Sequence↗
PubMedDate not supplied

Further compounds from the pedal gland of the bontebok (Damaliscus dorcas dorcas).

The identification of four further major constituents of the pedal gland exudate of the bontebok, Damaliscus dorcas dorcas, viz. alpha-terpineol, 2-n-heptylpyridine, m-cresol and (A)-6-dodecen-4-olide and the investigation of the stereochemistry of the double bond in (Z)-6-dodecen-4-olide by means of iterative computer analysis are described. An improved synthesis of this compound is outlined.

Animals↗
PubMedDate not supplied

Mammalian pheromone studies, VII. Identification of thiazole derivatives in the preorbital gland secretions of the grey duiker, Sylvicapra grimmia, and the red duiker, Cephalophus natalensis.

2-Isobutyl-1,3-thiazole and its 4,5-dihydro derivative were identified in the preorbital gland secretions of the grey duiker, Sylvicapra grimmia, and the red duiker, Cephalophus natalensis, but are absent from the preorbital secretion of the blue duiker, C. monticola. These two compounds which are present in high, but varying concentrations in the secretions of male grey duikers, are present in low concentrations in the secretions of females. This seems to be the only consistent significant difference between the secretions of male and female grey duikers and together with the fact that only males mark out their territories, was construed as evidence in favour of these two compounds playing a significant role in the territorial behaviour of male grey duikers.

Animals↗