id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-008480-p41oae8e	O'Callaghan, Barbara	Characterization of aminopeptidase N from Torpedo marmorata kidney	2004-11-12		.txt	text/plain	4411	263	53	Depending on solubilization conditions, both the antigen and peptidase activity were recovered either as a broad peak with a sedimentation coefficient of 18S (2% CHAPS) or as a single peak of 7.8S (1% CHAPS plus 0.2 % C(12)E(9)), showing that Torpedo aminopeptidase N behaves as an oligomer stabilized by hydrophobic interactions, easily converted into a 160 kDa monomer. The antigen is highly concentrated in the apical membrane of proximal tubule epithelial cells (600 gold particles/μm(2) of brush border membrane) whereas no labeling could be detected in other cell types or in other membranes of the same cells (basolatéral membranes, vacuoles or vesicles). Hybrids were selected in hypoxanthine, aminopterin and thymidine medium and superuatants from the culture wefts containing hybrid cells were tested for the presence of antibodies binding to the apical membrane of tubular epithelial cells on Torpedo kidney frozen sections.	./cache/cord-008480-p41oae8e.txt	./txt/cord-008480-p41oae8e.txt