title: [FTRaman and FTIR spectroscopy in lens with senile cataract].
abstract: OBJECTIVE
  In order to search for the main composition and conformational changes of lens proteins in senile cataract.
  
  
  METHODS
  We firstly used Fourier transform Raman and infrared (FTRaman and FTIR) spectroscopy and semi-quantitative method in the integral calculus of related peaks to determine the conformational changes of lens protein during opacification of varying grade.
  
  
  RESULTS
  The spectral features of lenses with grade III cataract were intermediate between human clear lenses (grade 0) and grade IV or grade V cataractous lenses. The spectral characteristics of lenses with grade IV were very similar to that with grade V lenses, and some peaks of them were not seen in human clear lenses. The two spectral analyses showed that some findings were identical and some findings were complementary.
  
  
  CONCLUSIONS
  The development of lens opacification is correlated not only with the relative contents of alpha-, beta-, gamma-crystallines in lens proteins but also with the various damaged SH, trp, phe, -CH2 in lens protein of senile cataract.
authors.affiliation: Beijing Eye Institute of Ophthalmology.
authors.forename: C
authors.initials: C
authors.lastname: Chen
authors.forename: X
authors.initials: X
authors.lastname: Su
authors.forename: X
authors.initials: X
authors.lastname: Zhang
mesh_terms: D000368:Aged; D002386:Cataract / Q000378:metabolism*; D003459:Crystallins / Q000032:analysis* / Q000737:chemistry; D005583:Fourier Analysis; D006801:Humans; D007908:Lens, Crystalline / Q000737:chemistry*; D008875:Middle Aged; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman / Q000379:methods
chemical_list: D003459:Crystallins