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Revised amino acid sequence, crystallization, and preliminary x-ray diffraction analysis of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii.

作者信息

Tomoo K, Ohishi H, Ishida T, Inoue M, Ikeda K, Aoki Y, Samejima Y

机构信息

Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.

出版信息

J Biol Chem. 1989 Feb 25;264(6):3636-8.

PMID:2914966
Abstract

The complete amino acid sequence of acidic Agkistrodon halys blomhoffii phospholipase A2 has been redetermined by a combination of manual and automatic Edman degradations. Acidic A. halys blomhoffi phospholipase is a single polypeptide chain consisting of 122 amino acids and is highly homologous in sequence with corresponding regions of phospholipase A2 from a variety of sources. Prism crystals of acidic A. halys blomhoffii phospholipase have been reproducibly grown from 2-methyl-2,4-pentanediol solution adjusted to pH 8.0 with 50 mM Tris-HCl buffer in the presence of 10 mM CaCl2. The crystals belong to space group P6(1)22 or P6(5)22 with hexagonal unit cell dimensions of a = b = 76.22 A and C = 76.56 A. One molecule occupies the asymmetric unit of the crystal. The diffraction extends to at least 2.5 A.

摘要

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