NDLI: Conformational stability of porcine serum transferrin.

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Conformational stability of porcine serum transferrin.

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Conformational stability of porcine serum transferrin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shen, Z. M. Wu, C. S. Feng, Y. M. Yang, J. T.
Description	Author Affiliation: Shen ZM ( Cardiovascular Research Institute, University of California, San Francisco 94143-0130.)
Abstract	The conformation of porcine serum ferric transferrin (Tf) and its stability against denaturation were studied by circular dichroism. Tf was estimated to have 19-24% alpha-helix and 50-55% beta-sheet based on the methods of Chang et al. (Chang, C.T., Wu, C.-S.C., & Yang, J.T., 1978, Anal. Biochem. 91, 13-31) and Provencher and Glöckner (Provencher, S.W. & Glöckner, J., 1981, Biochemistry 20, 33-37). Removal of the bound ferric ions (apo-Tf) did not alter the overall conformation, but there were subtle changes in local conformation based on its near-UV CD spectrum. The Tfs were stable between pH 3.5 and 11. Denaturation by guanidine hydrochloride (Gu-HCl) showed two transitions at 1.6 and 3.4 M denaturant. The process of denaturation by acid and base was reversible, whereas that by Gu-HCl was partially reversible. The irreversible thermal unfolding of Tfs began at temperatures above 60 degrees C and was not complete even at 80 degrees C. The bound irons (based on absorbance at 460 nm) were completely released at pH < 4 or in Gu-HCl solution above 1.7 M, when the protein began to unfold, but they remained intact in neutral solution even at 85 degrees C. The NH2- and COOH-terminal halves of the Tf molecule obtained by limited trypsin digestion had CD spectra similar to the spectrum of native Tf, and the COOH-terminal fragment had more stable secondary structure than the NH2-terminal fragment.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	1
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1992-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein Conformation Protein Structure, Secondary Transferrin Chemistry Animals Circular Dichroism Drug Stability Guanidine Guanidines Pharmacology Hydrogen-ion Concentration Metabolism Protein Denaturation Swine Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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