Sequence analysis of camel (Camelus dromedarius) lactoferrin

The aim of this study was to characterise camel lactoferrin in terms of pri mary structure and molecular weight. The protein was eluted from a heparin- sepharose column at a sodium chloride concentration of 0.5 M, and correspon ded to bovine lactoferrin in terms of N-terminal sequence and the molecular weight of 80.16-80.73 kDa. Lactoferrin cDNA was PCR amplified, using a cDN A library from lactating mammary gland of a Somali camel. The sequenced clo ne had a length of 2337 bp and an open reading frame of 2124 bp, which code d for a protein of 708 amino acid residues. The mature protein had a length of 689 amino acid residues, a calculated molecular weight of 75.250 kDa an d a calculated isoelectric point at pH 8.14. Primary structure identity to bovine lactoferrin was 74.9%. Concentration of lactoferrin in whole, late-l actational milk was 220 mg l(-1), which was higher than the lactoferrin con centration in comparable bovine milk, which was 140 mg l(-1). (C) 1999 Else vier Science Ltd. All rights reserved.