Literature DB >> 8740257

Possible changes in secondary structure and composition of human lens capsules in hereditary congenital cataract.

S M Lee1, S Y Lin, C L Cheng, R C Liang.   

Abstract

BACKGROUND: Scanty information is available on the changes in conformational structure and composition of human lens capsule in cases of hereditary congenital cataract. The purpose of this study was to use Fourier-transformed infrared (FT-IR) spectroscopy to determine the secondary structure and composition of hereditary cataractous human lens capsule, as compared with normal human lens capsule.
METHODS: FT-IR spectroscopy with the Fourier self-deconvolution and curve-fitting program was performed, and second-derivative analysis was used to verify the peak positions and assignments of the IR spectra.
RESULTS: The curve-fit FT-IR spectra revealed that the content of hydroxylysine and arginine were clearly higher in the lens capsule of the hereditary congenital patient, but the content of aspartic acid significantly lower, than in normal human lens capsules. The secondary conformational changes in alpha-helix, triple helix and random coil structures were important findings in the lens capsule of a hereditary cataractous patient.
CONCLUSION: Possible alterations in secondary structures and compositions of lens capsule are observed in the hereditary congenital cataractous patient by using FT-IR spectroscopy with curve-fitting and second-derivative analysis.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 8740257     DOI: 10.1007/bf00220711

Source DB:  PubMed          Journal:  Graefes Arch Clin Exp Ophthalmol        ISSN: 0721-832X            Impact factor:   3.117


  24 in total

1.  Ageing of the human corneal stroma: structural and biochemical changes.

Authors:  N S Malik; S J Moss; N Ahmed; A J Furth; R S Wall; K M Meek
Journal:  Biochim Biophys Acta       Date:  1992-03-20

2.  Association of hereditary cataracts in strain 13/N guinea-pigs with mutation of the gene for zeta-crystallin.

Authors:  Q L Huang; X Y Du; S H Stone; D F Amsbaugh; M Datiles; T S Hu; J S Zigler
Journal:  Exp Eye Res       Date:  1990-03       Impact factor: 3.467

3.  Investigations of protein structure with optical spectroscopy: bovine growth hormone.

Authors:  H A Havel; R S Chao; R J Haskell; T J Thamann
Journal:  Anal Chem       Date:  1989-04-01       Impact factor: 6.986

4.  Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter.

Authors:  J Alvarez; D C Lee; S A Baldwin; D Chapman
Journal:  J Biol Chem       Date:  1987-03-15       Impact factor: 5.157

5.  The lens capsule. Sugar and amino acid composition.

Authors:  S Fukushi; R G Spiro
Journal:  J Biol Chem       Date:  1969-04-25       Impact factor: 5.157

6.  Secondary conformational structure of type IV collagen in different conditions determined by Fourier-transform infrared microscopic spectroscopy.

Authors:  S M Lee; S Y Lin; R C Liang
Journal:  Artif Cells Blood Substit Immobil Biotechnol       Date:  1995

7.  Genetics of cataract.

Authors:  J François
Journal:  Ophthalmologica       Date:  1982       Impact factor: 3.250

8.  Characterization of peptide inducing cataractogenesis in lens of hereditary cataractous rat (ICR/f RAT).

Authors:  A Kamei; H Sakai
Journal:  Jpn J Ophthalmol       Date:  1989       Impact factor: 2.447

9.  Cross-linking in type IV collagen.

Authors:  A J Bailey; T J Sims; N Light
Journal:  Biochem J       Date:  1984-03-15       Impact factor: 3.857

10.  Early cytologic changes of Fraser cataract. An electron microscopic study.

Authors:  Y Hamai; T Kuwabara
Journal:  Invest Ophthalmol       Date:  1975-07
View more
  1 in total

1.  Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.

Authors:  Tianqi O Zhang; Ariel M Alperstein; Martin T Zanni
Journal:  J Mol Biol       Date:  2017-04-26       Impact factor: 5.469

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.