The purification and partial characterization of carp,Cyprinus carpio,vitellogenin |
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Authors: | Charles R Tyler John P Sumpter |
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Institution: | (1) Department of Biology and Biochemistry, Brunel University, Uxbridge, Middlesex, UB8 3PH, UK;(2) Dept. of Biology and Biochemistry, Brunel University, Uxbridge, Middx., UB8 3PH |
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Abstract: | A procedure is described for the isolation of intact vitellogenin (c-VTG) from the carp, Cyprinus carpio. VTG was induced in juvenile females using oestradiol-17β and purified from the plasma using a combination of gel-filtration
chromatography on Sepharose 6B and ion exchange chromatography on DEAE-cellulose. Purification procedures were conducted at
low temperatures (below 9°C) in the presence of the proteolytic enzyme inhibitor aprotinin to prevent degradation. Intact
c-VTG had an apparent molecular mass of 390,000 Daltons, but when extracted from plasma in the absence of aprotinin it underwent
proteolysis into at least 2 protein fragments (apparent molecular masses of 230,000 and 96,000 Daltons), showing an instability
of the native dimer. An amino acid analysis of c-VTG showed that its composition was almost identical to goldfish VTG, a species
closely allied to the true carps and also similar to other oviparous vertebrate VTGs. Collectively, these data indicate that
using these purification procedures VTG from carp, and probably other teleost species, can be isolated in an intact, highly
purified form. |
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Keywords: | carp vitellogenin purification |
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