Studies on the size and shape of rabbit intestinal glucoamylase-maltase complex.
Rabbit intestinal glucoamylase-maltase was examined in detail with respect to its molecular weight, sedimentation, diffusion and viscosity. It is a large asymmetrical molecule, with a molecular weight of 750 000-760 000. Its appearance under the electron microscope supports the idea that it is a long string (62.0 nm) consisting of eight beads of diameter 6.0 nm each and a surface-to-surface interbead distance of approx. 2.0 nm. The shape of the enzyme derived from its hydrodynamic behaviour by using the string-of-spherical-beads model originally proposed by Kuhn [(1932) Z. Phys. Chem. Abt. A 161, 1-32] and later modified by Shulman [(1953) J. Am. Chem. Soc. 75, 5846-5852] fits moderately well with the electron-microscopic picture. The beads might represent about six subunits, and the absence of sulphur from the enzyme and the inability to dissociate the enzyme by conventional methods indicate the possibility of unusual covalent cross-linking between the subunits and between the beads.
D000818:Animals; D005087:Glucan 1,4-alpha-Glucosidase; D005959:Glucosidases; D007421:Intestine, Small / Q000201:enzymology*; D008854:Microscopy, Electron; D008958:Models, Molecular; D008970:Molecular Weight; D009097:Multienzyme Complexes; D011487:Protein Conformation; D011817:Rabbits; D014461:Ultracentrifugation; D014783:Viscosity; D000520:alpha-Glucosidases
D009097:Multienzyme Complexes; D005959:Glucosidases; D000520:alpha-Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase