Structural Studies on Bovine Lactoferrin
نویسندگان
چکیده
منابع مشابه
Structural Studies on Bovine Growth Hormone
Purified bovine growth hormone, consisting of a single polypeptide chain, has been found to contain NHz-terminal alanine, phenylalanine, and methionine in nearly equal amounts. The minimum molecular weight calculated from its amino acid composition is 20,846. Five unique fragments have been prepared from bovine growth hormone by cleavage at 4 methionyl residues with cyanogen bromide. In the ord...
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ThirtyFrieswal lactating cows were screened for clinical and subclinical mastitis and subsequently classified into healthy, subclinically affected and clinically affected groups each group comprising of 10 cows. Polymorphism of cow lactoferrin (LTF) gene promoter was determined by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP). The results showed that LFT gene pro...
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The binding of lomefloxacin to bovine lactoferrin (BLf) in a dilute aqueous solution was studied using fluorescence spectra. The binding constant (K) and the number of binding sites (n) were obtained by a fluorescence quenching method. The binding distance (r) and energy-transfer efficiency (E) between lomefloxacin and bovine lactoferrin were also obtained according to the mechanism of Foörster...
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Lactoferrin (LF) is a well-known multifunctional protein. In this study, we report the inhibitory potency of bovine LF (bLF) on catechol-O-methyltransferase (COMT), which catalyzes methylation of catechol substrates. We found that bLF binds to and inhibits COMT using its N-terminal region. An N-terminal peptide fragment obtained from bLF by trypsin digestion showed a higher inhibitory activity ...
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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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63790-7