Intrinsic fluorescence characteristics of apomyoglobin adsorbed to microparticulate silica

C. H. Lochmüller, Steven S Saavedra

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The intrinsic fluorescence of sperm whale apomyoglobin was utilized as the probe in a study of protein adsorption, desorption, and conformational behavior on a series of microparticulate silica gels. The results indicate that adsorption is rapid and largely irreversible. The degree of protein unfolding that takes place upon adsorption is dependent on the pH of the contact buffer. The tryptophans in the pH 4.0 surface conformer are more exposed and interact to a greater extent with the interfacial environment than in the pH 7.5 surface conformer. Partial, reversible refolding of the protein in the sorbed state is observed with a change in the pH of the contact buffer.

Original languageEnglish (US)
Pages (from-to)433-438
Number of pages6
JournalLangmuir
Volume3
Issue number3
StatePublished - 1987
Externally publishedYes

Fingerprint

Silicon Dioxide
Fluorescence
Silica
silicon dioxide
Proteins
Adsorption
fluorescence
Buffers
proteins
adsorption
buffers
Silica Gel
Silica gel
whales
Tryptophan
tryptophan
Desorption
silica gel
desorption
apomyoglobin

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Intrinsic fluorescence characteristics of apomyoglobin adsorbed to microparticulate silica. / Lochmüller, C. H.; Saavedra, Steven S.

In: Langmuir, Vol. 3, No. 3, 1987, p. 433-438.

Research output: Contribution to journalArticle

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