CONSERVATION OF ARABIAN GAZELLES - Nwrc.gov.sa

Wildlife Research Center (KKWRC), near Riyadh, (25 0 03'N, 46 0 45'E). This Center is today in
charge of their captive propagation. From thi s group, 22 animals were karyotyped. Of these gazelles,
13 came from a private shop in Jeddah, five animals from NWRC, and four animals from private
collections in Taif. The precise origin of the gazelles from Jeddah is not known, but they were
collected from Aden (Yemen). The three founders of the NWRC nucleus were a gift from the Emir
of Naj ran (in south-west Saudi Arabia). Organs of two gazelles from NWRC were available for
protein electrophoresis.
Gazella gazella gazella: Tissue samples for electrophoresis were collected from 14
individuals from north em Israel. Eight animals were also sampled fo r cytogenetic studies. Organs
were sampled during controlled hunting organized by the Israeli Nature Reserve Authority to limit
overpopulation of gazelles.
Gazella gazella cora: Organs of two individuals originating from south-west Saudi Arabia
and kept at NWRC were taken for electrophoresis. Eight animals from the same region were also
karyotyped.
Gazella gazel/a Jarasani: Three animals from the Farasan Islands, a protected area located in
the Red Sea, were karyotyped.
Gazella subgutlurosa marica: Organs from five indi viduals bom at KKWRC were used for
protein electrophoresis. The KKWRC herd ori ginated from wild animals caught in different regions
of Saudi Arabia between 1976 and 1982. Fifty-eight gazelles from thi s population were karyotyped
(Granjon el al., 1991 ; Vassart el al. , 1993). The G-banded karyotype of G. s. marica is presented
here to allow comparison of banding pattems with G. gazella.
- Electrophoresis: Horizontal starch gel electrophoresis was performed on kidney, li ver and
heart samp les of G. g. gazella. G. g. erlangeri, G. g. cora and G. subgutturosa marica. Protein
extraction, electrophoresis, protein staining, and scori ng of the results were conducted according to
Pasteur el al. (I988). Twenty-four presumptive genetic loci were scored in all individuals. Buffers
used were tri s citrate pH 6.4,6.7 or 8.0 (TC), lithium hydroxide pH 8.3 (LiOH), tris maleate EOTA
pH 6.9 (TME), tris borate EDT A pH 8.6 (TBE) and tris HCI pH 8.5 (TH). The electrophoretic loc i
were identified with the foll owi ng format: enzyme, abbreviation, (Enzyme Commission Numbe r, and
buffer used). These included: adenylate kinase, AK. (E.C. 2.7.4.3, TC 6.4) from heart; alpha
glycerophosphate dehydrogenase, GPO, (E.C. 1.1.1.8, TC 8.0) from kidney; aspartate
aminotransferase, AA T, (E.C. 2.6.1.1, TME) from liver (2 loci); diaphorase, five esterases, ES, (E.C.
3.1.1, TME and TH) from liver; glycoxalase, GLO, (E.C. 4.4.1.5, LiOH) from kidney; glucose
phosphate isomerase, GPI, (E.C. 5.3. 1.9, TME) from liver; isocitrate dehydrogenase, IDH, (E.C.
1.1.1.42, TC 6.7) from kidney (2 loc i); lactate dehydrogenase, LOH, (E.C. 1.1.1.27, TC 6.7) from
kidney (2 loci); malate dehydrogenase, MOH, (E.C. 1.1.1.37, TC 6.7) from kidney (2 loci); mannose
phosphate isomerase, MPI, (E.C. 5.3.1.8, LiOH) from kidney; nucleoside phosphorylase, NP, (E.C.
2.4.2. 1, TME) from li ver; phosphoglucomutase, PGM, (E.C. 2.7.5.1, TME) from liver; sorbitol
dehydrogenase, SOH, (E.C. 1.1.1 .14, TC 8.0) from kidney; superoxide dismutase. SOD, (E.C.
1.15.1.1, LiOH) from kidney; 6-phosphogluconate dehydrogenase, 6PGO, (E.C. 1.1. 1.43, TC 6.7)
from kidney; and total proteins (TC 6.4) from heart. Percentage of polymorphic loci, mean number
of alleles per locus, and mean heterozygosities were calculated from allele frequencies. Nei and
Roger's genetic di stances were computed using the Phylip package of J. Felsenstein.
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