The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates.

The enzyme does not cleave β-linked galactose, as in lactose.

The lysosomal enzymes cleave the T from the iodinated thyroglobulin.

This enzyme then cleaves C5 to C5a, a potent anaphylatoxin, and C5b.

The angiogenesis inhibitor is generated when certain enzymes cleave it out of its parent plasminogen molecule.

The idea being that whenever the site was methylated, only the methylation insensitive enzyme could cleave at that position.

These enzymes cleave the N-terminus of the receptor, which in turn acts as a tethered ligand.

During HIV reproduction, the host cell's own enzymes cleave gp160 into gp120 and gp41.

Upon expression, the enzyme will cleave the plasmid at its corresponding recognition site creating sticky ends on the plasmid.

The enzyme would periodically cleave single bases, enabling the pore to identify successive bases.