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- Title
Human Milk Lactoferrin Hydrolyzes Ribonucleoside 5′-Triphosphates.
- Authors
Babina, S. E.; Semenov, D. V.; Buneva, V. N.; Nevinsky, G. A.
- Abstract
Lactoferrin (LF), one of the most important and polyfunctional factors of nonspecific cell defense against bacteria, viruses, and cancer diseases, is the main iron-transferring protein of human biological fluids, blood, and milk. Electrophoretically homogeneous preparations of LF from human milk were obtained and studied. Using chromatography on Blue Sepharose, LF preparations were separated into several subfractions differing in their affinity for the sorbent, two of which exhibited nucleoside 5-triphosphate-hydrolyzing activity. Using different methods, including in-gel ATPase activity assay, it was demonstrated that hydrolysis of ATP and other nucleotides is an intrinsic property of LF and that LF is the major ATPase of human milk. It is shown that the ATP-hydrolyzing center is located at the C-terminal domain of the LF molecule and that interaction between ATP and this center increases the oligonucleotide-hydrolyzing activity of the DNA-binding domain of this protein.
- Subjects
LACTOFERRIN; IRON proteins; BREAST milk; HYDROLYSIS; ALLOSTERIC proteins; DNA
- Publication
Molecular Biology, 2005, Vol 39, Issue 3, p452
- ISSN
0026-8933
- Publication type
Academic Journal
- DOI
10.1007/s11008-005-0061-5