Literature DB >> 2253478

Age-dependent variations in the camel lens crystallins.

A S Duhaiman1, M H Ismail.   

Abstract

1. Water-soluble crystallins from cortex and nucleus of both young and adult camel lenses were fractionated by gel filtration into high molecular weight aggregate (HMW-aggregate), alpha-low, beta-high, beta-low, gamma-high and gamma-low protein fractions. 2. Crystallins were characterized by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing (IEF). Changes related to age and lens parts were compared. 3. The major changes in crystallin distribution included an increase in HMW-aggregate (alpha-high), beta-high, and gamma, and a decrease in alpha-low and beta-low, when comparing lenses in the direction of the nucleus and in the direction of increasing age. 4. Similar changes were detected comparing either cortex and nucleus of the same lens or whole lenses of different age.

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Year:  1990        PMID: 2253478     DOI: 10.1016/0305-0491(90)90204-7

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  1 in total

1.  Glycation of human lens proteins from diabetic and (nondiabetic) senile cataract patients.

Authors:  A S Duhaiman
Journal:  Glycoconj J       Date:  1995-10       Impact factor: 2.916

  1 in total

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