Purification and Characterization of Camel Thyroglobulin |
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Authors: | Vijay Deshpande S.G. Venkatesh Torao Narita Mohammed Abdul Majid |
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Affiliation: | aDepartment of Biochemistry, University College of Science, Osmania University, Hyderabad–500 007, Andhra Pradesh, India;bLaboratory of Signal Transduction, Institute for Molecular and Cellular Regulation, Gunma University, 371, Maebashi, Japan;cDepartment of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Philadelphia, PA 19107-6799, USA |
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Abstract: | Thyroglobulin (669 kDa), the major protein of the camel thyroid, has been isolated and purified from saline extract of the gland by ammonium sulfate fractionation and DEAE-cellulose chromatography. Ultracentrifugal analysis of the purified material, with an iodine content of 0.39%, showed a major and minor component with S20,w values of 17 and 24, respectively. Separation of the protein from thyroid of individual animals by linear salt gradient on DEAE-cellulose showed a major and minor peak, indicating heterogeneity. Native gel electrophoresis of camel thyroglobulin showed a doublet, revealing microheterogeneity. A similar pattern was observed for the slower migrating components (24 S iodoprotein). N-terminal analysis of the purified protein revealed asparagine as the major N-terminal amino acid. Glycine and alanine were observed as the minor N-terminals. No differences in N-terminals between the major and minor peak were observed. Camel thyroglobulin, as thyroglobulin of other animal species, is a glycoprotein with a total carbohydrate content of 10.7%, comprising 6.0% neutral sugar, 3.67% glucosamine and 1.04% sialic acid. The iodoamino acid and amino acid composition of camel thyroglobulin is similar to that of other mammalian species. |
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Keywords: | Camel glycoprotein heterogeneity iodoprotein thyroglobulin triiodothyronine (T3) thyroxine (T4) |
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