Purification, crystallization, and X-ray diffraction studies of lactotransferrin from buffalo colostrum

Arch Biochem Biophys. 1992 Apr;294(1):319-21. doi: 10.1016/0003-9861(92)90175-v.

Abstract

Lactotransferrin is an iron-binding protein. It has been purified from buffalo colostrum. The purified lactotransferrin has been crystallized in 10% ethanol solution. The crystals are orthorhombic and the space group is P2(1)2(1)2(1) with unit cell dimensions a = 161.70 A, b = 155.75 A, c = 113.48 A. The asymmetric unit contains three molecules of the protein with a solvent content of about 59%. The crystals were stable in the X-ray beam and diffract beyond 3.5 A resolution. The native data have been collected and the structure determination is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Buffaloes*
  • Chemical Phenomena
  • Chemistry, Physical
  • Colostrum / chemistry*
  • Crystallization
  • Female
  • Lactoferrin / chemistry*
  • Lactoferrin / isolation & purification
  • X-Ray Diffraction

Substances

  • Lactoferrin