Literature DB >> 6405797

Studies on the fate of aldolase molecules in the aging rat lens.

A Dovrat, D Gershon.   

Abstract

It was found that aldolase activity declined considerably in the lens of adult animals with increasing age. Immunoassay showed that defective aldolase C molecules were accumulated. In addition, antibody prepared against denatured enzyme preferentially removes inactive molecules from lens homogenates without affecting active molecules. It is concluded that defective aldolase molecules encountered in aging lenses are at least partially denatured and are inactive.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6405797     DOI: 10.1016/0304-4165(83)90104-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  Counterpoint: The lens fluid circulation model--a critical appraisal.

Authors:  David C Beebe; Roger J W Truscott
Journal:  Invest Ophthalmol Vis Sci       Date:  2010-05       Impact factor: 4.799

2.  Localization of denatured enzyme molecules in rat lenses.

Authors:  J Scharf; A Dovrat; M Nahir
Journal:  Br J Exp Pathol       Date:  1988-06

3.  Identification of intracellular degradation intermediates of aldolase B by antiserum to the denatured enzyme.

Authors:  A Z Reznick; L Rosenfelder; S Shpund; D Gershon
Journal:  Proc Natl Acad Sci U S A       Date:  1985-09       Impact factor: 11.205

4.  Defective superoxide-dismutase molecules accumulate with age in human lenses.

Authors:  J Scharf; A Dovrat; D Gershon
Journal:  Graefes Arch Clin Exp Ophthalmol       Date:  1987       Impact factor: 3.117

5.  Reversal of age-related effects in rat muscle phosphoglycerate kinase.

Authors:  K C Yuh; A Gafni
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205

6.  Bacteriocuprein superoxide dismutases in pseudomonads.

Authors:  H M Steinman
Journal:  J Bacteriol       Date:  1985-06       Impact factor: 3.490

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.