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- W151483008 abstract "Growth of normal human lenses is maintained at a relatively constant rate of 0.4 mg per year after the first years of life. Water insoluble material increases at a similar constant rate, while the amount of water soluble components remains constant. Early growth stages’ are reflected by significant changes in relative abundance of all the major subunits in these fractions. However, from approximately age 40, the relative concentrations of the different subunits of lens proteins are fairly constant, except for a continued marked decrease in the 20,000 and increase in the 10,000 dalton water insoluble components. The relative stability in the concentrations of the polypeptides suggests that the rates of synthesis are comparable to the rates of degradation and/or insolubilization. The 10,000 dalton polypeptide is the result of degradation, probably of both soluble and insoluble 20,000 dalton components, which appears to be more rapid in the water insoluble fraction. The 43,000 dalton polypeptide is found in the water insoluble fraction of all ages; in the water soluble fraction, it only appears after the first few years of life, increasing until approximately age 30 at which time it is equivalent to that found in the insoluble fraction. Amino acid incorporation studies confirm the conclusion that the 43,000 dalton polypeptide is directly synthesized and the 10,000 dalton component arises by post-translational degradation. Ouabain causes differential inhibition, blocking almost completely the synthesis of polypeptides equal to or greater than 27,000 daltons. The decrease with aging of overall protein synthesis appears to occur at a uniform rate in the soluble cortical region at least in the 26 to 52 year-old age group." @default.
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- W151483008 date "1979-01-01" @default.
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- W151483008 title "A Preliminary Study of the Dynamic Aspects of Age Dependent Changes in the Abundances of Human Lens Polypeptides" @default.
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- W151483008 doi "https://doi.org/10.1007/978-94-009-9609-0_12" @default.
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