Ak. Sharma et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF MARE LACTOFERRIN, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1196-1198
Citations number
21
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Lactoferrin is an iron-binding glycoprotein with a molecular weight of
80 kDa. The protein has two iron binding sites. It has two structural
lobes, each housing one Fe3+ and the synergistic CO32- ion. The prote
in was isolated from the colostrum/milk of mares maintained at Nationa
l Research Centre on Equines, Hisar, India. The purified samples of th
e protein were crystallized using a microdialysis method. The protein
was dialysed against low ionic strength buffer solution. Several cryst
al forms were obtained, out of which three were characterized which ha
ve cell dimensions as follows. Form I a = 79.8, b = 103.5, c = 112.0 A
ngstrom, space group P2(1)2(1)2(1), with one protein molecule per asym
metric unit and a solvent content of 57%. Form II a = 84.9, b = 99.7,
c = 103.5 Angstrom, space group P2(1)2(1)2(1) with one molecule per as
ymmetric unit and a solvent content of 55%. Form III a = 151.0, b = 15
1.0, c = 240.6 Angstrom, space group P4(1)2(1)2 with three molecules i
n the asymmetric unit and a solvent content of 57%. The intensity data
up to 3.8 Angstrom resolution for form I, 2.9 Angstrom resolution dat
a for form II and 6 Angstrom resolution data for form III have been co
llected. Further calculations are in progress.