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

نویسندگان

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

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.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 264 6  شماره 

صفحات  -

تاریخ انتشار 1989