On the interaction of alpha-crystallin with membranes

The interaction of human and bovine alpha-crystallins with bovine lens membranes was evaluated using binding curves and Scatchard plots constructed from scans of SDS-PAGE gels and/or from the association of [14C]-leu alpha-crystallin with the membranes. No differences were observed for total bovine,...

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Bibliographic Details
Published inCurrent eye research Vol. 13; no. 3; p. 225
Main Authors Zhang, W Z, Augusteyn, R C
Format Journal Article
LanguageEnglish
Published England 01.03.1994
Subjects
Adult
Aged
Aged, 80 and over
Aging - physiology
Animals
Cataract - metabolism
Cattle
Cell Membrane - metabolism
Crystallins - isolation & purification
Crystallins - metabolism
Humans
Lens, Crystalline - metabolism
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Summary:The interaction of human and bovine alpha-crystallins with bovine lens membranes was evaluated using binding curves and Scatchard plots constructed from scans of SDS-PAGE gels and/or from the association of [14C]-leu alpha-crystallin with the membranes. No differences were observed for total bovine, normal human 19 and 88 year old and cataractous alpha-crystallins. In each case, interaction takes place through two distinct processes, a) a high affinity (Kd = 1 x 10(-8) M) binding with low capacity (25 mg alpha-crystallin/g membrane protein) and b) partitioning (Kp = 0.25 l/g membrane protein). Loss of the high-affinity binding component was observed for bovine nuclear alpha-crystallin. Contrary to previous reports, it is concluded that cataract formation does not affect the ability of human alpha-crystallins to interact with bovine lens membranes. Reanalysis of previously published data supports this conclusion.
ISSN:0271-3683
DOI:10.3109/02713689408995781