Revised amino acid sequence, crystallization, and preliminary x-ray diffraction analysis of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii.
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.
Tomoo
K
K
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
Ohishi
H
H
Ishida
T
T
Inoue
M
M
Ikeda
K
K
Aoki
Y
Y
Samejima
Y
Y
D000595:Amino Acid Sequence; D003435:Crotalid Venoms / Q000032:analysis*; D003460:Crystallization; D008969:Molecular Sequence Data; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
C031442:Agkistrodon venoms; D003435:Crotalid Venoms; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2