A-083 Performance evaluation of Sentinel Diagnostics' ACE assay on the Abbott Alinity c system and ARCHITECT c16000 System

The latter is converted to the potent vasoconstrictor, angiotensin II. ACE also inactivates bradykinin. Elevated levels of ACE activity occur in serum of ...

S Brambilla，C Assalini，E Frana，... - 《Clinical Chemistry》

A dipeptidyl carboxypeptidase that converts angiotension I and inactivates bradykinin.

The latter is converted to the potent vasoconstrictor, angiotensin II. ACE also inactivates bradykinin. Elevated levels of ACE activity occur in serum of ...

HYT Yang - 《Biochim.biopys.acta》

Serum Angiotensin Converting Enzyme Levels in Syphilis Patients

Angiotensin-converting enzyme (ACE), a dipeptidyl carboxypeptidase, hydrolyzes angiotensin I to the active angiotensin g and also inactivates bradykinin. Activity of ACE was first identified in plasrna by Skeggs et al in 1956. In 1975 Li...

JW Park，ES Park，JY Song

Biological inactivation of enkephalins and the role of enkephalin-dipeptidylcarboxypeptidase ("Enkephalinase") as neuropeptidase

Three types of well defined peptidase activities in CNS may account for the hydrolysis of the opioid pentapeptides : aminopeptidases, angiotensin-converting enzyme and enkephalin-dipeptidylcarboxypeptidase. The properties of these various enzyme...

Jean-Charles Schwartz，Bernard Malfroy，Sophie De La Baume - 《Life Sciences》

Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin...

Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II): studies with bradykinin ...

E Jaspard，L Wei，F Alhenc-Gelas - 《Journal of Biological Chemistry》

Biological inactivation of enkephalins and the role of enkephalin-dipeptidyl-carboxypeptidase (“enkephalinase”) as neuropeptidase

The weak and short-lasting biological activity of enkephalins can be ascribed to their rapid metabolism. Three types of well defined peptidase activities i...

Jean-Charles Schwartz and Bernard Malfroy and Sophie De La Baume - 《Life Sciences》