人唾液α-淀粉酶的结晶及初步X射线衍射研究

Crystallization and preliminary X-ray diffraction studies of human salivary alpha-amylase.

作者信息

Ramasubbu N, Bhandary K K, Scannapieco F A, Levine M J

机构信息

Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214.

出版信息

Proteins. 1991;11(3):230-2. doi: 10.1002/prot.340110308.

DOI:10.1002/prot.340110308

PMID:1749776

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.

摘要

非糖基化α-淀粉酶是人类腮腺唾液的主要成分，通过气相扩散技术，以2-甲基-2,4-戊二醇作为沉淀剂，在pH 9.0的氯化钙存在下进行结晶。晶体为正交晶系，空间群P2(1)2(1)2(1)，晶胞参数a = 53.3、b = 75.8和c = 138.1 Å。不对称单元包含一个淀粉酶分子。溶剂含量为54%。这些晶体对X射线稳定，衍射极限为2.8 Å，似乎适合进行X射线衍射研究。