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- Title
The Complete Primary Structure of α-Lactalbumin Isolated from Pig (Sus scrofa) Milk.
- Authors
GODOVAC-ZIMMERMANN, Jasminka; CONTI, Amedeo; NAPOLITANO, Lorenzo
- Abstract
The complete amino-acid sequence of pig α-lactalbumin has been determined. It was obtained by microsequencing of the native protein and the peptides derived after tryptic or cyanogen bromide cleavage. The tryptic peptides were separated by a rapid microbore HPLC method. Pig α-lactalbumin is 122 amino acids long and differs from the bovine homologue by 26 exchanged residues. Of the two prolines present in bovine α-lactalbumin, one has been deleted in the pig structure. All previously sequenced α-lactalbumins have shown glutamic acid at position 49, which is known to be the active site in the homologous lysozyme c structure. This residue is replaced by phenylalanine in pig α-lactalbumin indicating that the pig protein is the first α-lactalbumin with complete loss of all lysozyme functional residues.
- Publication
Biological Chemistry, 1990, Vol 371, Issue 2, p649
- ISSN
1431-6730
- Publication type
Article