Literature DB >> 6712681

Raman spectroscopic evidence for the microenvironmental change of some tyrosine residues of lens proteins in cold cataract.

A Mizuno, Y Ozaki, K Itoh, S Matsushima, K Iriyama.   

Abstract

Reversible "cold cataract" phenomenon of a SD-strain rat lens (29 days old) was studied by Raman spectroscopy in the temperature range of 35-17.5 degrees C. Cold cataract appeared in the lens nucleus below 26 degrees C. The Raman spectra did not show any detectable change in the 300-800 cm-1 and 900-4000 cm-1 regions as the temperature decreased. However lens opacification caused a significant change in the intensity ratio of tyrosine doublet near 840 cm-1, suggesting that some tyrosine residues in lens proteins undergo a change in their hydrogen bonding environment during the cold cataract formation. It was also found that the intensity ratio of the tyrosine doublet band provides a practical indicator of phase transition temperature of cold cataract.

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Year:  1984        PMID: 6712681     DOI: 10.1016/0006-291x(84)90871-4

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Visualization of crystallin droplets associated with cold cataract formation in young intact rat lens.

Authors:  W K Lo
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

2.  Signature molecular changes in the skeletal muscle of hindlimb unloaded mice.

Authors:  Muhammad Azeem; Rizwan Qaisar; Asima Karim; Anu Ranade; Adel Elmoselhi
Journal:  Biochem Biophys Rep       Date:  2021-01-29

Review 3.  Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.

Authors:  Megan A Rocha; Marc A Sprague-Piercy; Ashley O Kwok; Kyle W Roskamp; Rachel W Martin
Journal:  Chembiochem       Date:  2021-02-10       Impact factor: 3.164

  3 in total

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