Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase. |
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Authors: | N Ramasubbu K K Bhandary F A Scannapieco M J Levine |
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Institution: | Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214. |
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Abstract: | Nonglycosylated alpha-amylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2-methyl-2,4-pentanediol as the precipitant in the presence of CaCl2 at pH 9.0. The crystals are orthorhombic, space group P2(1)2(1)2(1) with unit cell dimensions of a = 53.3, b = 75.8, and c = 138.1 A. The asymmetric unit contains one amylase molecule. The solvent content is 54%. The crystals are stable to X-rays and diffract up to 2.8 A and appear to be suitable for X-ray diffraction studies. |
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Keywords: | parotid saliva enzyme crystals X-ray analysis |
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