A hydrophobic form of the small-intestinal sucrase-isomaltase complex.
作者： Hans Sigrist , Peter Ronner , Giorgio Semenza
DOI: 10.1016/0005-2736(75)90022-X
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摘要: Abstract A large scale preparation of brush border membranes is described. Solubilized by either papain or Triton X-100, the sucrase-isomaltase complex purified in a three-step procedure, including differential centrifugation, Sephadex G-200 and DEAE-cellulose chromatography. Detergent solubilized protease differ tendency to aggregate but not enzymatic characteristics. The chemical composition molecular weight two enzyme complexes are almost identical. Limited digestion Triton-solubilized produces protein electrophoretically indistinguishable from papain-solubilized together with low proteolytic fragments.
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