Lactoferrin (Lf), the major iron-binding component of milk, also a major constituent of the specific granules of neutrophils involved in antimicrobial activity and a glycoprotein thought to play a role in regulatory functions in the hematopoietic system as well as other physiologic activities, is shown to occur in three isoforms. One, Lf-alpha, binds iron; the other two, Lf-beta and Lf-gamma, express potent RNase activity, but do not bind iron. The three isoforms are very similar or identical in Mr, pI, partial proteolytic peptide patterns, NH2-terminal amino acid sequence, and reactivity with mAbs and polyclonal antisera against the RNase and Lf, respectively. The finding of structurally similar but enzymatically distinct forms of Lf may be related to the diverse functions of the molecule.
Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity.
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P Furmanski, Z P Li, M B Fortuna, C V Swamy, M R Das; Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity.. J Exp Med 1 August 1989; 170 (2): 415–429. doi: https://doi.org/10.1084/jem.170.2.415
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