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Preparation of protease free and rnase free pancreatic dnase ec 3.1.4.5


, : Preparation of protease free and rnase free pancreatic dnase ec 3.1.4.5. Journal of Biological Chemistry 253(20): 7216-7219

When pancreatic DNase I[EC 3.1.4.5] is used as a specific biochemical reagent in the preparation of nuclear RNA or nuclear proteins, freedom from contaminating RNases or proteases is an important property of the enzyme preparation. A simple 1-step procedure was developed to effect complete removal of trypsin, chymotrypsin and chymotrypsinogen by a combination of affinity chromatography and salting-out adsorption on lima bean protease inhibitor coupled to Sepharose (a column (0.9 .times. 60 cm) operated in series with a regeneratable 1 ml bed). Commercial preparations of DNase (about 10 mg) give a quantitative yield of the enzyme that is protease-free as evidenced by full stability for more than 10 days at pH 8 and 37.degree. C. Removal of the last traces of RNase was accomplished by affinity chromatography on a column (0.4 .times. 72 cm) of 5'-(4-aminophenyl-phosphoryl)-uridine 2'(3')-phosphate-Sepharose; the product is a highly active DNase that gives no detectable hydrolysis of RNA by assay on radioactive substrates.

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Lee S., 1988: Effects of pancreaticoduodenal allografts on diabetic testicular lesions in the rat. Abnormal testicular histology is common in untreated diabetic animals and men. Reversal of testicular lesions with return of function and fertility are seen in controlled diabetes. We investigated the effects of pancreaticoduodenal (PD) allografts...

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Dolphin A.C.; Scott R.H., 1989: Effects of gtp binding protein activation on l type calcium channel currents in cultured rat sensory and sympathetic neurons. Journal of Physiology (Cambridge) 410: 15P

Takahashi H., 1981: Purification and properties of coenzyme independent aldehyde dehydrogenase from the membrane fraction of acetobacter aceti. Coenzyme-independent aldehyde dehydrogenase was solubilized from the membrane fraction of A. aceti ssp. aceti with NaI. Since the enzyme was not bound to a cytochrome c-like component in this preparation, but formed an aggregate with other membran...

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