Gland thyroid

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OpenUrlAbstractStradling JR, Barbour C, Pitson DJ, et al. OpenUrlCrossRefPubMedWeb gland thyroid ScienceRyan CF, Lowe AA, Li D, et al. OpenUrlCrossRefPubMedWeb soil research ScienceChiner E, Sines-Costa J, Aiero LM, et al. Teschler H, Berthon-Jones M, Thompson AB, et al. UK Coronavirus (COVID-19) Guidance and support Home Research for Development Outputs Probing protein-tannin interactions by isothermal titration microcalorimetry.

From: Department for International Development Published 1 January 2003 Document Type: Journal Article Theme: Agriculture Authors: Mueller-Harvey, I. Contents Abstract Citation Links Abstract Isothermal titration microcalorimetry (ITC) has been gland thyroid to investigate protein-tannin interactions. Two hydrolyzable tannins were studied, namely myrabolan and tara Panretin (Alitretinoin)- Multum, for gland thyroid interaction gland thyroid bovine serum albumin (BSA), a model globular protein, and gelatin, a model proline-rich random coil protein.

Calorimetry data indicate gland thyroid protein-tannin interaction mechanisms are dependent upon the nature of the protein involved. Tannins bind to the random coil protein gelatin by a two-stage mechanism. The energetics of the gland thyroid stage show evidence for cooperative binding of tannins to gland thyroid protein, while the second stage indicates gradual saturation of binding sites as observed for interaction with BSA.

The structure and flexibility of the tannins themselves alters the stoichiometry of the interaction, but does not appear to have any significant affect on the overall binding mechanism observed. This study demonstrates the potential of ITC for providing an insight into the nature of protein-tannin interactions. Journal gland thyroid Agricultural and Food Chemistry (2003) 51 (18) 5189-5195.

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