A two-active site one-polypeptide enzyme: the isomaltase from sea lion small intestinal brush-border membrane. Its possible phylogenetic relationship with sucrase-isomaltase.
Open Access
- 1 April 1984
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (8) , 4878-4884
- https://doi.org/10.1016/s0021-9258(17)42927-9
Abstract
No abstract availableThis publication has 52 references indexed in Scilit:
- Purification and Characterization of a Pig Intestinal α‐Limit DextrinaseEuropean Journal of Biochemistry, 1983
- Sucrase-Isomaltase: A Stalked Intrinsic Protein of the Brush Border MembraneCritical Reviews in Biochemistry, 1983
- N‐terminal sequences of pig intestinal sucrase—isomaltase and pro‐sucrase—isomaltaseFEBS Letters, 1982
- Cell‐free synthesis of the one‐chain precursor of a major intrinsic protein complex of the small‐intestinal brush border membrane (pro‐sucrase—isomaltase)FEBS Letters, 1981
- The hydrophobic anchor of small‐intestinal sucrase—isomaltaseFEBS Letters, 1978
- Steady‐State Kinetics of Rabbit‐Intestinal SucraseEuropean Journal of Biochemistry, 1974
- Substructure of the myosin molecule: III. Preparation of single-headed derivatives of myosinJournal of Molecular Biology, 1973
- Intestinal glycosidase activities in congenitalmalabsorption of disaccbaridesThe Journal of Pediatrics, 1965
- Intestinal Disaccharidases: Absence in Two Species of Sea LionsScience, 1964
- Are the Pinnipedia Biphyletic?Systematic Zoology, 1960