id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-104272-lczm1z5z	Yusifov, Taleh N.	Tear lipocalin is the major endonuclease in tears	2008-01-29		.txt	text/plain	4121	244	54	To determine the mode of hydrolysis, the cleaved ends of the DNA digested by tear DNases were analyzed by 3′ and 5′ end labeling using either terminal deoxynucleotidyl transferase or polynucleotide kinase with or without pretreatment with alkaline phosphatase. Both are Mg(2+) dependent enzyme endonucleases that are enhanced by Ca(2+), active at physiologic pH, inhibited by aurintricarboxylic acid, and catalyze hydrolysis of DNA to produce 3′-OH/5′P ends. Both endonucleases in tears show maximal activity in hydrolyzing plasmid DNA in 50 mM NaCl (Figure 4 ). To compare the DNA fragment sizes remaining after hydrolysis by TL and the minor endonuclease, dideoxy sequencing gel electrophoresis was performed on the digestion products ( Figure 9 ). The size variation of the final single strand hydrolysis products observed in sequencing gels for DNase I, TL, and the minor endonuclease may reflect mechanistic interactions of the DNA substrate with unique binding and cleavage sites.	./cache/cord-104272-lczm1z5z.txt	./txt/cord-104272-lczm1z5z.txt