 Reference Base  Major adenohypophyseal proteins of Indian rhinoceros (Rhi... |
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Nath, n.c., 1994. Major adenohypophyseal proteins of Indian rhinoceros (Rhinoceros unicornis). Indian Journal of Animal Sciences 64: 482-484, figs. 1-2
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| Location: |
Captive - Asia |
| Subject: |
Physiology |
| Species: |
Indian Rhino |
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Biometry of pituitary and polyacrylamidegel (7% and 10%) clectrophoretic pattern of anterior pituitary proteins of Indian rhinoceros, a species about which there is little information, are presented in this paper.
Three rhinoceros calves, 1 male (9 days old) and 2 females (3 and 4 months old respectively) separated from their mothers because of floods were shifted from the Kaziranga National Park to the State Zoo-cum-Botanical Garden, Assam. The calves died due to gastroenteritis. Their pituitaries were collected immediately after death. The pituitary gland was flat and triangular (Fig. 1), weighing 0.44 ? 0.04 mg (? SE). The brown anterior pituitary covered the pale posteriorpituitaryalmostentirelyandformed the major portion (0.35 ? 0.03 mg) of the gland. The mean length, breadth and thickness of the whole pituitary gland were 1.10 ?0.06,1.20 ? 0.06 and 0.67 ? 0.07 mm respectively. The gross anatomy of pituitary of Indian rhinoceros was comparable to that of horse (Venze 1977).
Alkaline extract (0.1 M ammonium bicarbonate, pH8.6) of fresh anterior pituitary tissue of Indian rhinoceros calves and cow (bovine) were prepared (Nath and Singh 1992). Polyacrylamide-gel (7 and 10%) electrophoresis of pituitary proteins was performed in a tube (10 cm X 0.5 cm) using Lds (hydroxymethyl) methylamine glycine buffer (0.0.4M, pH 8.6) as described by Davis (1964). Pituitary protein (200 pg) was applied for electrophoresis. Electrophoresis was performed at a constant current of 1 mA/gel tube for 15 min and then increased to 3 mA/ gel tube (200-250 V) for 2 br till tracking dye (bromophenol blue, 0.05%) reached the lower end of the gel. The gels were stained with 1 % amido black in 7% acetic acid. Destaining was done by several changes of 7% acetic acid.
The electrophoretic pattern of major anterior pituitary protein of bovine has been studied previously (NaLh and Singh 1992) using standard bovine GH and bovine PRL from the National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases, Baltimore, Maryland, USA. Two major bands corresponding to GH and PRL were seen in both 7 and 10% gel (Fig. 2). The separation of 2 PRL bands in rhinoceros was not very distinct compared to the bovine. In 7% gel the relative mobility of GH for calves 9 days and and 3-4 months old were 0.27 and 0.34-, in 1 0% gel they were 0.22 and 0.26 respectively. These mobilities in case of PRL were 0.72 (9 days) and 0.67 (3-4 months) for 7% gel, and 0.47 (9 days) and 0.42 (3-4 months) for 10% gel. Some minor protein bands were also observed in 3 and 4 months old calves. One minor protein band having electrophoretic mobility intermediate to GH and PRL was seen. This protein band was named as albumin (Sinha and Baxter 1979, Talamantes et a]. 198 1) or albumin-like protein (Nath and Singh 1992) in many other species of animals due to same molecular weight as of serum albumin (66 kd). One or two minor protein bands moving just ahead of GH and PRL were also observed in standard bovine GH and PRL (Nalh and Singh 1992) and in freshlyprepared anterior pituitary alkaline tissue homogenatc of many species of animals (Russel et al. 1978, Nath and Singh 1992). Russel et al. (1978) and Talamantes et al. (1981) claimed that these doublets are probably deaminated forms of GH and PRL. These minor protein hmds were not observed in the anterior pituitary protein of 9-day-old rhinoceros calf. Probably the absence of deaminated forms of GH and PRL in 9-day-old calf caused the difference in the electrophoretic mobility with that of calves 3-4 months old. The clectrophoretic mobility of protein at aluine pH was inversely related to pI values of protein. Molecular changes such as deamination or substitution of charged for an unchanged amino acid side chain would also induce such changes in pI and electrophoretic mobility (Wallis 1973).
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