Preferential interaction among lens proteins as evidenced from accessibility of crystallins to ammonia gas

Frederick A. Bettelheim, J. Samuel Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

Different crystallins (α, βH, βL and low molecular weight-LMW) were isolated from bovine lenses. The study of accessibility of the lyophilized solid proteins to ammonia gas was conducted in a high-vacuum vapor sorption apparatus. The sorption and desorption isotherms obtained were used to calculate the sorptive capacity and retentive capacity (hysteresis and irreversibly sorbed ammonia gas) of the different proteins. Individual crystallins were used to study the accessibility of the self-aggregates. Protein mixtures (βH + βH; α + LMW, etc.) were employed to study the accessibility of binary, tertiary and finally quaternary systems to ammonia vapor. Finally lyophilized thin sections of the bovine lenses were exposed to ammonia vapor. Comparing the sorptive and retentive capacities of self- and hetero-aggregates gave an indication of the preferred interactions among lens proteins in free solution, and by inference in situ, in the lens fibers.

Original languageEnglish (US)
Pages (from-to)227-236
Number of pages10
JournalExperimental eye research
Volume47
Issue number2
DOIs
StatePublished - Aug 1988

Keywords

  • accessibility
  • chemisorption
  • crystallin
  • lens
  • molecular aggregates

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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