DNase I and cu-amylase are commercial products obtained from mammalian sources and may be separated from contaminating RNase by treatment. with bentonite. The completeness of RNase removal is demonstrated by using a highly sensitive technique employing E. coli ribosomal RKA as substrate.
Standard preparations of ribonuclease crystals of modifications I and II
โ Scribed by Murray Vernon King
- Publisher
- Elsevier Science
- Year
- 1964
- Weight
- 316 KB
- Volume
- 79
- Category
- Article
- ISSN
- 0926-6577
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โฆ Synopsis
Detailed methods are described for preparation of bovine pancreatic ribonuclease (polyribonucleotide 2-ofigonucleotidotransferase (cyclizing), EC 2.7.7.16 ) crystals of Modifications I and II of quality suitable for X-ray diffraction studies. The reasons for choice of solvent and buffer systems are discussed, especial regard being paid to the use of the solvent 2-methyl-2,4-pentanediol and to the application of preserving solutions as media for handling the crystals after growth. Some necessary precautions are specified.
๐ SIMILAR VOLUMES
Preparation, crystal and molecular structure of aquadichlorocaffeinecopper(II), determined by threedimensional X-ray data, are reported. The darkish green crystals are orthorhombic, space group P212121 with cell dimensions: a = 16.370(9), b = 13.432(7), c = 5.814(6) a and Z = 4. The structure was so
## Abstract For Abstract see ChemInform Abstract in Full Text.
The reaction of W 6 Br 12 with CuBr sealed in an evacuated silica tube at the temperature gradient 925/915 K and annealing at 625/300 K yields a mixture of orthorhombic ฮฑ-Cu 2 [W 6 Br 14 ] and cubic b-Cu 2 [W 6 Br 14 ] in the low temperature zone. ฮฑ-Cu 2 [W 6 Br 14 ] crystallizes in the space group