Journal ArticleDOI
The use of 1-anilino Naphthalene-8-sulfonate (ANS) for studying the effects of iodination on thyroglobulin conformation.
TLDR
The findings of the present work are consistent with the hypothesis that thyroglobulin is arranged in similar or even identical structural domains and that iodination gradually modulates the protein conformation.About:
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1981-11-01. It has received 15 citations till now. The article focuses on the topics: Organification & Iodine.read more
Citations
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Journal ArticleDOI
The earliest site of iodination in thyroglobulin is residue number 5.
TL;DR: It is demonstrated that of nearly 70 tyrosyl residues present in rat thyroglobulin, there is one, residue number 5 from the NH2-terminal end, which has in vivo the highest affinity toward iodine, being the first one to be iodinated.
Journal ArticleDOI
Antigenic determinants on thyroglobulin: comparison of the reactivities of different thyroglobulin preparations with serum antibodies and T cells of patients with chronic thyroiditis.
TL;DR: It appears that the Tg-reactive T cells predominantly recognize determinants on the T g molecule that are unrelated to hormone-containing sites, and variations in Tg conformation related to iodination of the molecule do not contribute significantly to its reactivity with autoantibodies and T cells.
Journal ArticleDOI
A nonincinerative rate-sensing method for the determination of iodine in iodoproteins.
TL;DR: This procedure is proposed as a simple process for the sensitive determination of the iodine in iodoproteins without separation or the need for alkaline or acid digestion.
Journal ArticleDOI
Chemically Modified Human Immunoglobulin G: Hydrophobicity and Surface Activity at Air/Solution Interface.
TL;DR: The modified IgGs decrease surface tension at the air/solution interface more effectively than the native protein and influence of the overall IgG hydrophobicity and the length of the attached alkyl chain on the dimensions of the mobile protein segment at the surface are discussed.
Journal ArticleDOI
Chemically Modified Glucose Oxidase with Enhanced Hydrophobicity: Adsorption at Polystyrene, Silica, and Silica Coated by Lipid Monolayers
Alexander Kamyshny,A Feldman,Adam Baszkin,M.M. Boissonnade,Véronique Rosilio,Shlomo Magdassi +5 more
TL;DR: Covalent modification of glucose oxidase from Aspergillus niger by the palmitic acid ester of N-hydroxysuccinimide at a molar ratio ester:protein of 56:1 results in the formation of the enzyme derivative with 11 attachedpalmitic chains, which displays a much higher adsorption affinity for hydrophilic and hydrophobic surfaces.
References
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Journal ArticleDOI
The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites
TL;DR: In this paper, anilino-8-naphthalene sulfonate (ANS) was used as a fluorescent probe of non-polar regions in proteins and its fluorescence changes markedly when it is bound to the apoprotein.
Journal ArticleDOI
The determination of sugar in blood and spinal fluid with anthrone reagent
TL;DR: The authors' procedure for the determination of dextran to the estimation of the sugar in blood and spinal fluid is adapted, and a stabilized anthrone reagent has been developed, and certain findings of interest are reported.
Journal ArticleDOI
Fluorescence Spectroscopy of Proteins
TL;DR: Fluorescence spectroscopy of proteins, analyzing polarity, distances between groups, flexibility and conformational transitions, and its applications in medicine and materials science.
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Fragmentation of bovine serum albumin by pepsin. i. the origin of the acid expansion of the albumin molecule.
Gregorio Weber,Lorna B. Young +1 more
Journal ArticleDOI
Negative cooperativity in the binding of thyroxine to human serum prealbumin
TL;DR: It is evident that the binding of T4 represents a case of negative cooperativity which is presumably due to interaction between ligands.
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