Ft-ir study on the hydration of calcium bilirubinates

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

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish (US)
Pages (from-to)413-414
Number of pages2
JournalProceedings of SPIE - The International Society for Optical Engineering
Volume1145
DOIs
StatePublished - Dec 1 1989
Externally publishedYes

Fingerprint

Hydration
Calcium
Bilirubin
Linking
hydration
calcium
Molecules
Water
Glycoproteins
Glycoprotein
Swelling
pigments
Skeleton
musculoskeletal system
Conformation
Pigments
Salt
swelling
water
Conformations

ASJC Scopus subject areas

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

Cite this

Ft-ir study on the hydration of calcium bilirubinates. / Guo, H.; Soloway, R. D.; Yang, Z.; Ding, X.; Xu, D.; Wu, J.

In: Proceedings of SPIE - The International Society for Optical Engineering, Vol. 1145, 01.12.1989, p. 413-414.

Research output: Contribution to journalArticle

Guo, H. ; Soloway, R. D. ; Yang, Z. ; Ding, X. ; Xu, D. ; Wu, J. / Ft-ir study on the hydration of calcium bilirubinates. In: Proceedings of SPIE - The International Society for Optical Engineering. 1989 ; Vol. 1145. pp. 413-414.
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