Purification, crystallization, and X-ray diffraction studies of lactotransferrin from buffalo colostrum.
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.
Raman
A
A
Department of Biophysics, All India Institute of Medical Sciences, New Delhi.
Bhatia
K L
KL
Singh
T P
TP
Srinivasan
A
A
Betzel
C
C
Malik
R C
RC
D000818:Animals; D002020:Buffaloes; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003126:Colostrum / Q000737:chemistry*; D003460:Crystallization; D005260:Female; D007781:Lactoferrin / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D007781:Lactoferrin