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| Content Provider | Springer Nature Link |
|---|---|
| Author | Massucci, Maria Teresa Giansanti, Francesco Di Ni, Giovanna Turacchio, Mala Giardi, Maria Federica Botti, Dario Ippoliti, Rodolfo De Giulio, Barbara Sicilia, Rosa Donnarumma, Giovanna Valenti, Piera Bocedi, Alessio Polticelli, Fabio Ascenzi, Paolo Antonini, Giovanni |
| Copyright Year | 2004 |
| Abstract | Bovine lactoferrin catalyzes the hydrolysis of synthetic substrates (i.e., Z-aminoacyl-7-amido-4-methylcoumarin). Values of Km and kcat for the bovine lactoferrin catalyzed hydrolysis of Z-Phe-Arg-7-amido-4-methylcoumarin are 50 μM and 0.03 s−1, respectively, the optimum pH value is 7.5 at 25 °C. The bovine lactoferrin substrate specificity is similar to that of trypsin, while the hydrolysis rate is several orders of magnitude lower than that of trypsin. The bovine lactoferrin catalytic activity is irreversibly inhibited by the serine-protease inhibitors PMSF and Pefabloc. Moreover, both iron-saturation of the protein and LPS addition strongly inhibit the bovine lactoferrin activity. Interestingly, bovine lactoferrin undergoes partial auto-proteolytic cleavage at positions Arg415-Lys 416 and Lys440-Lys441. pKa shift calculations indicate that several Ser residues of bovine lactoferrin display the high nucleophilicity required to potentially catalyze substrate cleavage. However, a definitive identification of the active site awaits further studies. |
| Starting Page | 249 |
| Ending Page | 255 |
| Page Count | 7 |
| File Format | |
| ISSN | 09660844 |
| Journal | BioMetals |
| Volume Number | 17 |
| Issue Number | 3 |
| e-ISSN | 15728773 |
| Language | English |
| Publisher | Kluwer Academic Publishers |
| Publisher Date | 2004-01-01 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Physical Chemistry Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences |
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