id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-104282-90t1m430	nan	Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids	1994-09-02		.txt	text/plain	7076	394	53	Abbreviations used in this paper: CAT, chloramphenicol acetyltransferase; FP2, NADPH-cytochrome P-450 reductase; msALDH, microsomal aldehyde dehydrogenase; PBS(+), PBS containing 1 mM CaCI2 and 0.5 mM MgCI2; PDI, protein disulfide isomerase; PTP, protein tyrosine phosphatase; STE, sucrose solution containing 10 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10 t~g/ml leupepdn A, 0.5 mM PMSF, and 10 U/ml Trasyol; SRP, signal recognition particle. The nucleotide sequence predicts a polypeptide of 484 amino acids, and the most characteristic feature of this membrane-bound ALDH is carboxyl-terminal 35 amino acids, consisting of a stem region (amino acids 450-463) and a hydrophobic domain (amino acids 464-480) followed by a short hydrophilic tail region (amino acids 481-484) as shown in Fig. 1 . These data, together with those from subcellular fractionation, suggested that the carboxyl-terminal portion of msALDH including the hydrophobic sequence (amino acid 464-480) was necessary for both its ER localization and the tight association with the ER membrane.	./cache/cord-104282-90t1m430.txt	./txt/cord-104282-90t1m430.txt