July 1987
Volume 28, Issue 7
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Articles  |   July 1987
Inhibition of beta-crystallin cross-linking in the Ca2+-treated lens.
Investigative Ophthalmology & Visual Science July 1987, Vol.28, 1218-1222. doi:
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      L Lorand, S M Conrad, P T Velasco; Inhibition of beta-crystallin cross-linking in the Ca2+-treated lens.. Invest. Ophthalmol. Vis. Sci. 1987;28(7):1218-1222.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

beta-Crystallin dimers of approximately 55,000 weight are among the early products of protein cross-linking in Ca2+-treated rabbit lens, caused by the activation of intrinsic transglutaminase; formation of the cross-linked species can be blocked by 75 mM histamine (Lorand et al, Biochemistry, 24:1525-1531, 1985). As an extension of this work, we initiated a search for more specific inhibitors of cross-linking in this system. Of the compounds tested so far, hydroxylamine, methoxyamine, bisaminoxypropane and aminoacetonitrile were particularly effective, inhibiting the generation of the cross-linked dimer in the 5 to 10 mM concentration range during a 4 hr treatment of the lens with Ca2+-ions.

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