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• W1993262490 abstract "Sucrose was used to simulate the dense in vivo environment during the extraction and isolation of soluble proteins (crystallins) from the cortical and nuclear regions of the calf lens. Addition of sucrose to the eluting buffer markedly affects the βH-crystallin region during gel filtration with Sepharose 6B-CL in a Tris buffer alone: the region is progressively diminished by levels of 0·25 m and 0·50 m-sucrose and disappears completely in buffered 1·0 m-sucrose. Concomitantly, decreases in the βH-crystallin region are accompanied by increases in the βL-crystallin region of the chromatogram developed with the Tris buffer alone. Compared to 10% of the total weight of proteins that elute as γ-crystallin in Tris buffer, only 3% are recovered in the presence of 0·25 m-sucrose. A poorly resolved peak immediately preceding the γ-crystallin region and a small increase in α-crystallin are observed with 1·0 m-sucrose. The changes in the crystallins were further characterized and demonstrated by equilibrium ultracentrifugation as well as by polyacrylamide gel electrophoreses in the presence and absence of urea. Weight average molecular weights (Mw) determined in Tris buffer containing 1·0 m-sucrose used for isolation of the three major cortical crystallin fractions gave values of 840 000, 55 000 and 23 500 daltons. They correspond, respectively, to those for α-, βL- and γ-crystallins isolated with Tris buffer alone. Results from gel electrophoresis in 7·0 m-urea indicate that the β-crystallin fraction isolated in 1·0 m-sucrose contains the sum of polypeptides present in βH- and βL-crystallins. In the absence of urea, however, polyacrylamide gel pattern of the native, undissociated sucrose β-crystallin fraction is distinetly different from and cannot be accounted for by a combination of those of βH- and βL-. With or without urea present the gel patterns for α- and γ-crystallin fractions isolated in buffered 1·0 m-sucrose are indistinguishable from those for the respective crystallins obtained in the Tris buffer alone. The observed changes in βH- and γ-crystallins upon the introduction of sucrose are shown to be reversible upon the removal of the reagents. These results suggest that the interaction or aggregation of lens proteins in a dense medium of reduced activity of water is different from that in a dilute buffer." @default.
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• W1993262490 date "1978-11-01" @default.
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• W1993262490 title "Effects of sucrose on interactions of calf lens soluble proteins" @default.
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• W1993262490 doi "https://doi.org/10.1016/0014-4835(78)90140-9" @default.
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