Properties of a Heparin-binding Peptide Derived from Bovine Lactoferrin
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چکیده
منابع مشابه
The Identification of a Novel Peptide Derived from Lactoferrin Isolated from Camel Milk with Potential Antimicrobial Activity
Background and Objective: Antimicrobial peptides have attracted significant attention in recent decades because of their properties, such as rapid bactericidal effects, having a wide spectrum of activity, and a rare development of drug resistance. The purpose of this study was to examine the antibacterial activity of a peptide derived from the lactoferrin isolated from camel milk against Staphy...
متن کاملAntibacterial activity in bovine lactoferrin-derived peptides.
Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified, one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf, one differing from Lf-cin B by t...
متن کاملIdentification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein.
Bovine and human lactoferrins (LF) prevent hepatitis C virus (HCV) infection in cultured human hepatocytes; the preventive mechanism is thought to be the direct interaction between LF and HCV. To clarify this hypothesis, we have characterized the binding activity of LF to HCV E2 envelope protein and have endeavored to determine which region(s) of LF are important for this binding activity. Seve...
متن کاملPhospholipid binding properties of bovine prothrombin peptide residues 1-45.
The present study investigates the unique contribution of the NH2-terminal 33 residues of prothrombin, the gamma-carboxyglutamic acid (Gla) domain, to the Ca(II) and phospholipid-binding properties of prothrombin. Two Gla domain peptides, 1-42 and 1-45, produced by chymotryptic cleavage of prothrombin fragment 1 (residues 1-156 of the amino terminus of bovine prothrombin) and isolated by anion-...
متن کاملLactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin.
Rat mast cell protease 1 (RMCP-1) is a secretory granule serine protease (chymase) that is recovered in vivo in a macromolecular complex with heparin proteoglycan (PG). We have previously shown that heparin activates RMCP-1 and that RMCP-1, when bound to heparin PG, is largely resistant to inhibition by a variety of macromolecular protease inhibitors. In the search for alternative mechanisms in...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1998
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(98)75843-6