Optimization of Thyroglobulin Coated Tube for Thyroglobulin IRMA Kit
نویسندگان
چکیده
منابع مشابه
The Properties of Thyroglobulin VIII. THE IODINATION OF THYROGLOBULIN
It has been shown that when thyroglobulin is iodinated, a marked intensification occurs in its absorption spectrum in the region of 300 to 3fXl rnp in alkaline solution (1). It is also well known that the absorption peaks of iodinated tyrosine and thyronine derivatives occur in this spectral zone (2). A procedure based on these factors has been developed which permits the simultaneous determina...
متن کاملSubunit heterogeneity of thyroglobulin.
The subunit structure of thyroglobulin has been investigated by gel filtration and polyacrylamide electrophoresis in sodium dodecyl sulfate (SDS) of the native and the S-carboxymethylated proteins. When the thyroglobulins from several species (calf, sheep, pig, man, rat, and guinea pig) were examined by polyacrylamide electrophoresis in SDS in the absence of reducing agents, most of the protein...
متن کاملELISA for thyroglobulin in serum: recovery studies to evaluate autoantibody interference and reliability of thyroglobulin values.
An ELISA for measuring thyroglobulin (Tg) in serum was developed with polyclonal antibodies to Tg on the solid phase and two monoclonal antibodies to Tg as the second antibodies. The assay has a detection limit of 1 microgram/L, a within-run imprecision (CV) of <7%, and a between-run CV of < 10%. Parallelism of the assay was shown in dilution studies, in which the percent observed/expected valu...
متن کاملPolypeptide chain composition of thyroglobulin.
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...
متن کاملThe Ultrastructure of Human Thyroglobulin
Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the molecule was estimated to be 110 A. The pitch varied between 40 and 50 A. Thyroglobulin molecules d...
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ژورنال
عنوان ژورنال: JKPK (Jurnal Kimia dan Pendidikan Kimia)
سال: 2018
ISSN: 2503-4154,2503-4146
DOI: 10.20961/jkpk.v3i2.22400