Topographical Relationship between Sucrase and Leucine β-Naphthylamidase on the Microvilli Membrane of Rabbit Intestinal Mucosal Cells
- 1 March 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 79 (3) , 479-488
- https://doi.org/10.1093/oxfordjournals.jbchem.a131091
Abstract
The topographical relationship between sucrase [EC 3. 2.1.26] and leucine β-naphthyl-amidase (LNAase) on the microvilli membrane of rabbit small-intestinal mucosal cells was studied assuming that where enzymes with different antigenicities, A and B, are situated in close proximity on the surface of microvilli vesicles, the agglutination of vesicles by anti-A antibody is inhibited by the previous binding of monovalent fragments of anti-B antibody to enzyme B on the surface of vesicles. Like anti-sucrase antibody, anti-LNAase antibody quantitatively agglutinated microvilli vesicles. It inhibited the membrane-bound LNAase activity in the same manner as the deter-gent-solubilized activity. This inhibitory effect of anti-LNAase antibody was not interfered with by monovalent fragments of anti-sucrase antibody. However, the monovalent fragments inhibited vesicle agglutination by anti-LNAase antibody as well as by anti-sucrase antibody. These results indicate that LNAase is located on the outer surface of microvilli vesicles and suggest that LNAase and sucrase are situated in close proximity on the membrane surface of microvilli vesicles.This publication has 1 reference indexed in Scilit:
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951