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- W2029467820 abstract "Triton-solubilized sucrase from rabbit intestine was examined by negative-staining electron microscopy. It has the dimeric structure in which two subunits similar in shape and size (about 45 × 65 Å) are united to each other at their long axes. In aqueous solution a certain number (10–15 in most cases) of the enzyme molecules gather together to form an aggregate usually 400 to 435 Å in diameter, in which they align radially around a core, the identity of which is unknown at present. Neither of Triton-solubilized sucrase digested by papain nor papain-solubilized sucrase forms any aggregates. The detergent-solubilized sucrase is adsorbed on the hydrophobic surface of fragmented polystyrene latex, and the adsorbed sucrase is released by papain. These results indicate that the Triton-solubilized sucrase has a hydrophobic portion at or near an end of its elongated molecule. Anti-sucrase immunoglobulin G and monovalent fragments from it bind to the aggregate and enlarge its diameter by at most 120 Å." @default.
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- W2029467820 date "1978-01-01" @default.
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- W2029467820 title "Electron microscope studies on triton-solubilized sucrase from rabbit small intestine" @default.
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- W2029467820 doi "https://doi.org/10.1016/s0022-5320(78)80026-4" @default.
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