On the hydrophobic part of aminopeptidase and maltases which bind the enzyme to the intestinal brush border membrane

Abstract

The intestinal brush border aminopeptidase and unfractionated maltases M2+M3 are composed of a hydrophilic, sugar containing and enzymatically active part, and a smaller hydrophobic part presumably binding the catalytic part of the lipid matrix of the membrane. Hydrophobic parts detaced by trypsin from the detergent forms of aminopeptidase and the maltases were purified and shown to have molecular weights ranging from 8000 to 10000. All are rich in hydrophobic residues and contain no disulfide bridges. However, their overall amino acid composition is different. The hydrophobic parts appear to be N-terminal in the detergent forms of the enzymes.