PEPTIDASES IN HUMAN BLOOD

Peptidases in human blood. I. The hydrolysis of glycylglycine and glycyl-L-leucine by normal serum.

Ever since peptidases were shown to be present in serum, various theories have been proposed to explain the origin and the mode of release of these enzymes (14). A thorough study of the properties of various serum peptidases has, however, not been made; instead, most investigators have tacitly assumed that the serum enzymes behave in a manner analogous to that of the known peptidases isolated f...

Inhibition of peptidases in the control of blood pressure.

The natriuretic peptide and renin-angiotensin systems are physiological counterparts with opposite roles in the regulation of electrolyte balance and blood pressure. In both systems, membrane-bound, zinc-dependent peptidases play an important role in the inactivation or activation of the system. Angiotensin-converting enzyme (ACE) converts angiotensin I into angiotensin II, and neutral endopept...

Zymogram studies of human intestinal brush border and cytoplasmic peptidases.

Zymogram studies of peptide hydrolases from the human intestinal brush border and cytoplasmic fractions produced multiple bands--that is, up to seven--while the brush border membrane produced only a single band of enzyme activity. With all of the substrates tested except L-leucyl-L-leucyl-L-leucine, a band having anodic mobility identical with that produced by the brush border enzymes was produ...

Signal peptidases.

Activation profiles of human kallikrein-related peptidases by matrix metalloproteinases.

The 15 human kallikrein-related peptidases (KLKs) are clinically important biomarkers and therapeutic targets of interest in inflammation, cancer, and neurodegenerative disease. KLKs are secreted as inactive pro-forms (pro-KLKs) that are activated extracellularly by specific proteolytic release of their amino-terminal pro-peptide, and this is a key step in their functional regulation. Physiolog...