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Age-related variations in the distribution of crystallins within the bovine lens
- Source :
- Experimental Eye Research. 43:1019-1030
- Publication Year :
- 1986
- Publisher :
- Elsevier BV, 1986.
-
Abstract
- The native water-soluble proteins of equator, anterior cortex, posterior cortex and nucleus from bovine lenses in the age range 0·3–33·7 years were analyzed by high-pressure gel-permeation chromatography and high-pressure ion-exchange chromatography. Unlike the equator and cortices, the nucleus shows a gradual decrease in α-crystallin proportion with age which is not compensated for by an increase in HM-crystallin. The β H 6 -crystallin species, almost the only β H -component in the youngest lens, is largely replaced by at least four fractions with higher and lower molecular weights in the older lenses. In the nucleus a β L -component (39 000 MW) increasingly seems to replace the major β L -crystallin ( β L 2 , 50 000 MW). Moreover, a switch in the synthesis of monomeric crystallins is demonstrated. This study clearly reveals an age-related increase in the size heterogeneity of the native soluble crystallins with age.
- Subjects :
- Aging
Biology
High-performance liquid chromatography
Cellular and Molecular Neuroscience
Crystallin
Age related
medicine
Animals
Distribution (pharmacology)
Molecular mass
Bovine lens
Lens Nucleus, Crystalline
Lens Cortex, Crystalline
Anatomy
Chromatography, Ion Exchange
Crystallins
eye diseases
Sensory Systems
Molecular Weight
Ophthalmology
medicine.anatomical_structure
Anterior cortex
Chromatography, Gel
Biophysics
Cattle
sense organs
Nucleus
Subjects
Details
- ISSN :
- 00144835
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- Experimental Eye Research
- Accession number :
- edsair.doi.dedup.....9d46586a1edcd0bedf0b9743582d1b41