June 1974
Volume 13, Issue 6
Free
Articles  |   June 1974
Some Enzymic Properties of Human Lens Esterase I
Author Affiliations
  • ARNOLD A. SWANSON
    College of Medicine, Department of Biochemistry, Medical University of South Carolina, 80 Bane St., Charleston, S. C. 29401
  • ANN W. TRUESDALE
    College of Medicine, Department of Biochemistry, Medical University of South Carolina, 80 Bane St., Charleston, S. C. 29401
Investigative Ophthalmology & Visual Science June 1974, Vol.13, 466-468. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      ARNOLD A. SWANSON, ANN W. TRUESDALE; Some Enzymic Properties of Human Lens Esterase I. Invest. Ophthalmol. Vis. Sci. 1974;13(6):466-468.

      Download citation file:


      © ARVO (1962-2015); The Authors (2016-present)

      ×
  • Supplements
This content is PDF only. Please click on the PDF icon to access.
Abstract

Lens esterase I was purified 23 times from normal lenses to apparent homogeneity as judged by chromatography on DEAE Sephadex and isoelectric focusing. Optimum rates of hydrolysis were observed at pH 6.8. The substrates of choice were α-naphthyl acetate, butyrate, caproate, caprylate, and β-propionate. The esterase shows an isoelectric point of 5.1 and a Km value of 0.095 mM with a-naphthyl acetate at pH 6.8. Enzymic activity was stimulated by the addition of either Ca+2 or Mn+2. The hydrolysis of substrates was inhibited by EDTA, phenylmethylanesulphonyl fluoride, p-hydroxy mercuribenzoate, diisopropylfiuorophosphate, diethyl-β-nitrophenyl phosphate, and urea.

×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×