Literature DB >> 3581874

Lactate dehydrogenase activity and its isoenzymes in concentric layers of adult bovine and calf lenses.

D Sempol, E Osinaga, S Zigman, I Korc, B Korc, A Sans, R Radi, J C Berretta, A Cayota, M Schwalb.   

Abstract

The activity of lactate dehydrogenase (LDH) and its isoenzyme pattern were studied in four concentric layers of adult bovine and calf lenses. In both groups the specific activity of the total LDH diminished progressively toward the internal nuclear layer; the decrease was greater in the adult lenses. The enzyme activities in the cortical layers of the calf lens were lower than in the adult lens, but in the inner nuclear layers, the opposite was found. All of the 5 LDH isoenzymes were found in each layer. In both groups of animals the LDH1 isoenzyme prevailed, followed by LDH2. No differences were found in the percentage of each isoenzyme in the different lens layers. The differences in the activitie(s) of LDH found may be due to post-translational or post-synthetic modifications which may occur during the aging process.

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Year:  1987        PMID: 3581874     DOI: 10.3109/02713688709025213

Source DB:  PubMed          Journal:  Curr Eye Res        ISSN: 0271-3683            Impact factor:   2.424


  1 in total

1.  Topographical distribution of lactate dehydrogenase activity in human clear eye lenses and in lenses with different types of senile cataract: a histochemical investigation.

Authors:  H Pau; H G Hartwig; R Fassbender
Journal:  Graefes Arch Clin Exp Ophthalmol       Date:  1997-10       Impact factor: 3.117

  1 in total

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