Age-related changes in the polypeptide composition of β-crystallin from bovine lens

J. Samuel Zigler

doi:10.1016/0014-4835(78)90063-5

Age-related changes in the polypeptide composition of β-crystallin from bovine lens

J. Samuel Zigler

School of Medicine

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

β_H-Crystallin and β_L-crystallin were isolated from bovine lenses of widely varying age. Electrophoretic analysis of the disaggregated polypeptide chains demonstrated marked age-related shifts in relative polypeptide abundance, both among the polypeptides common to β_H and β_L and those unique to β_H. The data suggest the possibility that post-synthetic modifications may occur in bovine β-crystallin, as has previously been shown for bovine α-crystallin.

Original language	English (US)
Pages (from-to)	537-546
Number of pages	10
Journal	Experimental eye research
Volume	26
Issue number	5
DOIs	https://doi.org/10.1016/0014-4835(78)90063-5
State	Published - May 1978

Keywords

age-related changes
electrophoresis
lens proteins
long-lived proteins
polypeptide composition
post-synthetic modifications
β-crystallin

ASJC Scopus subject areas

Ophthalmology
Sensory Systems
Cellular and Molecular Neuroscience

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10.1016/0014-4835(78)90063-5

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title = "Age-related changes in the polypeptide composition of β-crystallin from bovine lens",

abstract = "βH-Crystallin and βL-crystallin were isolated from bovine lenses of widely varying age. Electrophoretic analysis of the disaggregated polypeptide chains demonstrated marked age-related shifts in relative polypeptide abundance, both among the polypeptides common to βH and βL and those unique to βH. The data suggest the possibility that post-synthetic modifications may occur in bovine β-crystallin, as has previously been shown for bovine α-crystallin.",

keywords = "age-related changes, electrophoresis, lens proteins, long-lived proteins, polypeptide composition, post-synthetic modifications, β-crystallin",

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year = "1978",

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AU - Zigler, J. Samuel

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AB - βH-Crystallin and βL-crystallin were isolated from bovine lenses of widely varying age. Electrophoretic analysis of the disaggregated polypeptide chains demonstrated marked age-related shifts in relative polypeptide abundance, both among the polypeptides common to βH and βL and those unique to βH. The data suggest the possibility that post-synthetic modifications may occur in bovine β-crystallin, as has previously been shown for bovine α-crystallin.

KW - age-related changes

KW - electrophoresis

KW - lens proteins

KW - long-lived proteins

KW - polypeptide composition

KW - post-synthetic modifications

KW - β-crystallin

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JO - Experimental eye research

JF - Experimental eye research

IS - 5

ER -

Age-related changes in the polypeptide composition of β-crystallin from bovine lens

Abstract

Keywords

ASJC Scopus subject areas

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