Crystallization and preliminary X‐ray diffraction studies of human salivary α‐amylase

Proteins: Structure, Function and Bioinformatics - Tập 11 Số 3 - Trang 230-232 - 1991
N. Ramasubbu1,2, K. K. Bhandary1, Frank A. Scannapieco1, M.J. Levine1
1Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, New York 14214
2Department of Oral Biology, Foster Hall, School of Dental Medicine, State University of New York, Buffalo, NY 14214‐3092

Tóm tắt

AbstractNonglycosylated α‐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 P212121 with unit cell dimensions of a = 53.3, b = 75.8, and c = 138.1 Å. 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 Å and appear to be suitable for X‐ray diffraction studies.

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Tài liệu tham khảo

10.1016/B978-0-12-011507-5.50007-0

Boackle R., 1980, The Biologic Basis of Dental Caries, 113

10.1016/0003-9969(87)90024-0

Yamashita K., 1980, Structural studies of the sugar chains of human parotid α‐amylase, J. Biol. Chem., 255, 5635, 10.1016/S0021-9258(19)70676-0

10.1016/0003-9861(70)90446-7

10.1016/0003-9969(83)90003-1

Scannapieco F. A., 1989, Characterization of salivary α‐amylase binding to Streptococcus sanguis, Infect. Immun., 57, 2853, 10.1128/iai.57.9.2853-2863.1989

10.1016/S0006-291X(05)80900-3

10.1177/00220345900690110701

10.1016/0378-1119(86)90110-1

10.1007/BF00257032

10.1093/oxfordjournals.jbchem.a134659

10.1021/bi00478a019

10.1002/j.1460-2075.1987.tb02731.x

10.1098/rstb.1981.0069

10.1007/BF01024888

10.1042/bj2590145

Curby W. A., 1953, Device for collection of parotid saliva, J. Lab. Clin. Med., 41, 493

McPherson A., 1982, Preparation and Analysis of Protein Crystals., 82

Gribskov C. L., 1989, Improved crystallization by vapor diffusion, Am. Cryst. Assn. Abstracts, Ser 2, Poster Abstracts No. 49, 17, 90

10.1107/S002188988708662X

10.1016/0022-2836(68)90205-2

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Thông tin xuất bản

Proteins: Structure, Function and Bioinformatics

Tập 11 Số 3

230-232

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