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Cloning and sequencing of the porcine lactoferrin cDNA
Author(s) -
ALEXANDER L. J.,
LEVINE W. B.,
TENG C. T.,
BEATTIE C. W.
Publication year - 1992
Publication title -
animal genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.756
H-Index - 81
eISSN - 1365-2052
pISSN - 0268-9146
DOI - 10.1111/j.1365-2052.1992.tb00137.x
Subject(s) - lactoferrin , complementary dna , biology , cloning (programming) , amino acid , peptide sequence , microbiology and biotechnology , cysteine , biochemistry , glycosylation , protein sequencing , cdna library , gene , enzyme , computer science , programming language
Summary. cDNA clones encoding the entire porcine lactoferrin protein were isolated and sequenced. The porcine lactoferrin cDNA sequence presented here is 2259 bp in length and encodes a leader peptide of 19 amino acids and a mature protein of 684 amino acids. Comparisons with other lactoferrins indicate a single glycosylation site. The iron‐ and anion‐binding sites, and the cysteine residues involved in disulphide bonds, are conserved between the lactoferrin proteins.