Structural stability of glycophorin. Effects of heat and guanidine · HCl

David M. Byers; Jacob A. Verpoorte

doi:10.1016/0005-2795(78)90393-8

Structural stability of glycophorin. Effects of heat and guanidine · HCl

David M. Byers, Jacob A. Verpoorte

Medicine

Medicine

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

The effects of guanidine hydrochloride and high temperature on human glycophorin and sialic acid-free glycophorin were monitored by circular dichroism, viscosity, and fluorescence of 1-anilino-8-naphthalane sulfonate (ANS). The following observations were made: 1. 1.|Glycophorin and its sialic acid-free counterpart are unusually stable to both guanidine · HCl and heat. 2. 2.|CD and viscosity measurements indicate that guanidine · HCl neither causes a cooperative unfolding nor generates a random coil. 3. 3.|The ANS binding site is much more sensitive to guanidine · HCl than the ellipticity at 220 nm (θ₂₂₀). 4. 4.|The effect of temperature on CD is reversible whereas the effect of guanidine · HCl is not. 5. 5.|The carbohydrate moiety influences the viscosity, and also contributes to the changes in θ₂₂₀ when solutions of glycophorin are heated. These unusual properties indicate a complex mechanism of unfolding for this structurally stable macromolecule.

Original language	English
Pages (from-to)	478-486
Number of pages	9
Journal	BBA - Protein Structure
Volume	533
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(78)90393-8
Publication status	Published - Apr 26 1978

Bibliographical note

Funding Information:
We thank Dr. M. Gorelick of the Canadian Red Cross for the generous supply of blood cells, Mrs. R. Breckon for technical assistance and Dr. A.H. Blair for Helpful discussions. This study was supported by a grant from the Medical Research Council of Canada.

ASJC Scopus Subject Areas

General Medicine

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title = "Structural stability of glycophorin. Effects of heat and guanidine · HCl",

abstract = "The effects of guanidine hydrochloride and high temperature on human glycophorin and sialic acid-free glycophorin were monitored by circular dichroism, viscosity, and fluorescence of 1-anilino-8-naphthalane sulfonate (ANS). The following observations were made: 1. 1.|Glycophorin and its sialic acid-free counterpart are unusually stable to both guanidine · HCl and heat. 2. 2.|CD and viscosity measurements indicate that guanidine · HCl neither causes a cooperative unfolding nor generates a random coil. 3. 3.|The ANS binding site is much more sensitive to guanidine · HCl than the ellipticity at 220 nm (θ220). 4. 4.|The effect of temperature on CD is reversible whereas the effect of guanidine · HCl is not. 5. 5.|The carbohydrate moiety influences the viscosity, and also contributes to the changes in θ220 when solutions of glycophorin are heated. These unusual properties indicate a complex mechanism of unfolding for this structurally stable macromolecule.",

author = "Byers, {David M.} and Verpoorte, {Jacob A.}",

note = "Funding Information: We thank Dr. M. Gorelick of the Canadian Red Cross for the generous supply of blood cells, Mrs. R. Breckon for technical assistance and Dr. A.H. Blair for Helpful discussions. This study was supported by a grant from the Medical Research Council of Canada.",

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AU - Verpoorte, Jacob A.

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PY - 1978/4/26

Y1 - 1978/4/26

N2 - The effects of guanidine hydrochloride and high temperature on human glycophorin and sialic acid-free glycophorin were monitored by circular dichroism, viscosity, and fluorescence of 1-anilino-8-naphthalane sulfonate (ANS). The following observations were made: 1. 1.|Glycophorin and its sialic acid-free counterpart are unusually stable to both guanidine · HCl and heat. 2. 2.|CD and viscosity measurements indicate that guanidine · HCl neither causes a cooperative unfolding nor generates a random coil. 3. 3.|The ANS binding site is much more sensitive to guanidine · HCl than the ellipticity at 220 nm (θ220). 4. 4.|The effect of temperature on CD is reversible whereas the effect of guanidine · HCl is not. 5. 5.|The carbohydrate moiety influences the viscosity, and also contributes to the changes in θ220 when solutions of glycophorin are heated. These unusual properties indicate a complex mechanism of unfolding for this structurally stable macromolecule.

AB - The effects of guanidine hydrochloride and high temperature on human glycophorin and sialic acid-free glycophorin were monitored by circular dichroism, viscosity, and fluorescence of 1-anilino-8-naphthalane sulfonate (ANS). The following observations were made: 1. 1.|Glycophorin and its sialic acid-free counterpart are unusually stable to both guanidine · HCl and heat. 2. 2.|CD and viscosity measurements indicate that guanidine · HCl neither causes a cooperative unfolding nor generates a random coil. 3. 3.|The ANS binding site is much more sensitive to guanidine · HCl than the ellipticity at 220 nm (θ220). 4. 4.|The effect of temperature on CD is reversible whereas the effect of guanidine · HCl is not. 5. 5.|The carbohydrate moiety influences the viscosity, and also contributes to the changes in θ220 when solutions of glycophorin are heated. These unusual properties indicate a complex mechanism of unfolding for this structurally stable macromolecule.

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Structural stability of glycophorin. Effects of heat and guanidine · HCl

Abstract

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