PURIFICATION, CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF MARE LACTOFERRIN

Citation
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
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1196 - 1198
Database
ISI
SICI code
0907-4449(1996)52:<1196:PCAPCA>2.0.ZU;2-E
Abstract
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.