id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-006553-0rmuvb5i	Lew, Rebecca A.	Characterization of Angiotensin Converting Enzyme-2 (ACE2) in Human Urine	2006-05-05		.txt	text/plain	2930	121	50	A soluble form of ACE, generated by proteolytic cleavage of the membrane-bound form, has been shown to be present in urine; although evidence for a similar release of ACE2 has been reported in cell culture, it is not yet known whether this occurs in vivo. Ang II is generated by two successive enzymatic steps: first, an inactive decapeptide (Ang I) is liberated from a liver-derived protein angiotensinogen by the aspartic protease renin in the circulation; the active eightresidue Ang II peptide is then formed by the action of the membrane-bound metallopeptidase, angiotensin converting enzyme (ACE). Like a number of membrane proteins, ACE has been shown to be proteolytically released from the cell surface (Parkin et al., 2004) , resulting in the presence of a catalytically active form circulating through the bloodstream, as well as in other biological fluids, including urine and seminal plasma (Hooper, 1991) .	./cache/cord-006553-0rmuvb5i.txt	./txt/cord-006553-0rmuvb5i.txt