Ft-ir study on the hydration of calcium bilirubinates

H. Guo; R. D. Soloway; Z. Yang; X. Ding; D. Xu; J. Wu

doi:10.1117/12.969526

Ft-ir study on the hydration of calcium bilirubinates

H. Guo, R. D. Soloway, Z. Yang, X. Ding, D. Xu, J. Wu

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Abstract

Comparison of the dessicated and hydrated forms of the neutral salt of calcium bilirubinate indicated that water alters both the C-E1 skeleton and the polar groups of the molecule, suggesting that water may considerably alters the conformation and, therefore, the properties of calcium bilirubinate. The small degree of swelling indicates that some cross-linking is present in this ionic polymer but that it is much less than in whole pigment gallstones, suggesting that other molecules, possibly glycoproteins, provide much of the cross-linking.

Original language	English (US)
Pages (from-to)	413-414
Number of pages	2
Journal	Proceedings of SPIE - The International Society for Optical Engineering
Volume	1145
DOIs	https://doi.org/10.1117/12.969526
State	Published - Dec 1 1989
Externally published	Yes

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics
Computer Science Applications
Applied Mathematics
Electrical and Electronic Engineering

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abstract = "Comparison of the dessicated and hydrated forms of the neutral salt of calcium bilirubinate indicated that water alters both the C-E1 skeleton and the polar groups of the molecule, suggesting that water may considerably alters the conformation and, therefore, the properties of calcium bilirubinate. The small degree of swelling indicates that some cross-linking is present in this ionic polymer but that it is much less than in whole pigment gallstones, suggesting that other molecules, possibly glycoproteins, provide much of the cross-linking.",

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T1 - Ft-ir study on the hydration of calcium bilirubinates

AU - Guo, H.

AU - Soloway, R. D.

AU - Yang, Z.

AU - Ding, X.

AU - Xu, D.

AU - Wu, J.

PY - 1989/12/1

Y1 - 1989/12/1

N2 - Comparison of the dessicated and hydrated forms of the neutral salt of calcium bilirubinate indicated that water alters both the C-E1 skeleton and the polar groups of the molecule, suggesting that water may considerably alters the conformation and, therefore, the properties of calcium bilirubinate. The small degree of swelling indicates that some cross-linking is present in this ionic polymer but that it is much less than in whole pigment gallstones, suggesting that other molecules, possibly glycoproteins, provide much of the cross-linking.

AB - Comparison of the dessicated and hydrated forms of the neutral salt of calcium bilirubinate indicated that water alters both the C-E1 skeleton and the polar groups of the molecule, suggesting that water may considerably alters the conformation and, therefore, the properties of calcium bilirubinate. The small degree of swelling indicates that some cross-linking is present in this ionic polymer but that it is much less than in whole pigment gallstones, suggesting that other molecules, possibly glycoproteins, provide much of the cross-linking.

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JO - Proceedings of SPIE - The International Society for Optical Engineering

JF - Proceedings of SPIE - The International Society for Optical Engineering

ER -

Ft-ir study on the hydration of calcium bilirubinates

Abstract

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