Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography.

Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Research Abstract Details 

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Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Abstract Text:

K Mizuno,T Hayashi,

Type I collagen in phosphate-buffered saline (PBS) bound to a heparin-Sepharose column, while heat-treated type I collagen, denatured chains of alpha 1(I) and alpha 2(I), did not. Conformation-dependent association of type I collagen with heparin was further examined in various urea concentrations. The relative amount of bound fraction decreased in proportion to the concentration of added urea; from over 90% in the absence of urea to about 30% in 3 M urea, although circular dichroism spectrum of type I collagen was not changed by the presence of 4 M urea at 25 degrees C. In 2 M urea, the relative amount of bound fraction was about 50%. Rechromatography of the flow-through fraction or bound fraction of type I collagen in 2 M urea after lyophilization showed a similar pattern to that of the initial type I collagen solution in that about a half of either sample was recovered as bound fraction. This result indicated that the association potential of type I collagen with heparin appeared to have changed reversibly. The relative amount of bound fraction was little affected by the initial protein concentration, suggesting that intermolecular interaction between type I collagen molecules or the aggregate possibly resulting from the interaction is not important in the affinity with heparin. From these results, we suggest that triple-helical type I collagen molecules undergo reversible changes of conformation in urea solution between the conformation with heparin affinity and that without the affinity. In contrast, type V collagen or alpha1 (V) chain binds to heparin under the same conditions and therefore the conformational change of type V collagen in urea solution would not be discernible in terms of heparin affinity, even if the type V collagen molecules have altered conformation in urea, as is suggested for type I collagen.

Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Publishing Authors By Initials

K Mizuno,T Hayashi,

For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

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Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 116

Page Numbers: 1257-63

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1994

Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Keywords Mesh Terms:

KEYWORDS: Urea

MESH TERMS: chemistry

Chemical & Substance for Abstract: Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography. Information

Substance Name: Sepharose

Registry Number: 9012-36-6

Grant and Affiliation Information for Peculiar effect of urea on the interaction of type I collagen with heparin on chromatography.

AFFILIATION: Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo.

Country: JAPAN

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MEDLINETA: J Biochem

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