Identification of 1,1′-Bi(4-anilino)naphthalene-5,5′-disulfonic Acid Binding Sequences in α-Crystallin

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Binding of γ-crystallin substrate prevents the binding of copper and zinc ions to the molecular chaperone α-crystallin.

α-Crystallin is a small heat shock protein and molecular chaperone. Binding of Cu2+ and Zn2+ ions to α-crystallin leads to enhanced chaperone function. Sequestration of Cu2+ by α-crystallin prevents metal-ion mediated oxidation. Here we show that binding of human γD-crystallin (HGD, a natural substrate) to human αA-crystallin (HAA) is inversely related to the binding of Cu2+/Zn2+ ions: The high...

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PURPOSE alpha-Crystallin is the major protein of the mammalian lens where it contributes to the refractive properties needed for vision and possibly to the stability of the tissue. The aim of this study was to determine whether the properties of alpha-crystallin have changed during the course of evolution. METHODS Dogfish alpha-crystallin, which appeared over 420 million years ago, has been c...

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1,3-Disulfonic acid imidazolium hydrogen sulfate {[Dsim]HSO4} as a highly efficient, recyclable and green catalyst for the preparation of α,α´-bis(arylidene)cycloalkanones

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Brdtain N - Terminal Sequences of a - Crystallin

The amino acid sequences at the N-terminal ends of the chains of the lens protein, a-crystallin, were studied. Both the main kinds of chain in bovine ix-crystallin (A chains and B chains) have an N-terininal methionine residue, and the amino group is acetylated. Selective purification of the peptides in a tryptic digest of bovirne a-crystallin gave a preparation consisting largely of the N-term...

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Understanding the α-crystallin cell membrane conjunction

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1998

ISSN: 0021-9258

DOI: 10.1074/jbc.273.25.15474