Thyroglobulin structure-function. Isolation and characterization of a thyroxine-containing polypeptide from bovine thyroglobulin.
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چکیده
منابع مشابه
Thyroglobulin structure-function. Isolation and characterization of a thyroxine-containing polypeptide from bovine thyroglobulin.
Upon reduction and alkylation, 19 S bovine thyroglobulin gave rise to a family of polypeptides ranging in molecular weight from 10,000 to 330,000. T h i s group of polypeptides has been fractionated by chromatography on agarose gel in 6 M urea. After observing significantly increased iodine and thyroxine contents in the lowest molecular weight fraction obtained from the agarose gel-6 M urea chr...
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It is known that thyroglobulin can be dissociated into a component which appears to be a half molecule (12 S) of the undissociated molecule (19 S). In the present work, these two molecular species were isolated with a high degree of purity by preparative gel electrophoresis in sodium dodecyl sulfate and were individually reduced. The reduction pattern of the 12 S form displayed only two closely...
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Although thyroglobulin (Tg), the thyroid prohormone, is well known as a T cell dependent autoantigen in human and experimental autoimmune thyroid disease, very little is known about the molecular basis of Tg recognition by T cells. In this paper, we have characterized the epitopes recognized by two clonotypically distinct, murine Tg autoreactive T cell hybridomas, CH9 and ADA2. In vitro iodinat...
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1. Glycopeptides were isolated by gel filtration on Sephadex G-25 and Sephadex G-50 from a Pronase digest of porcine thyroglobulin. 2. Isolated glycopeptides were separated into five main fractions on a column of DEAE-Sephadex A-25. Of these fractions I to III were further purified by SE-Sephadex C-25 or DEAE-Sephadex A-25 column chromatography. Several of the purified glycopeptides were homoge...
متن کاملCharacterization of a hormonogenic domain from human thyroglobulin.
A polypeptide domain of molecular mass near 22 kDa was purified from CNBr-digest of iodine poor human thyroglobulin (hTgb). This fragment represents the N-terminal part of the hTgb molecule and consequently contains the preferential hormonogenic tyrosine 'acceptor' of the protein. This fragment could correspond to the non-iodinated and unreduced form of the thyroxinyl-containing 26 kDa peptide ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68778-8