Two Apparent Molecular Forms of Bovine Lactoferrin
نویسندگان
چکیده
منابع مشابه
Association of Bovine Lactoferrin Gene with Mastitis in Frieswal Cattle
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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Tryptic hydrolysis of galactosyltransferase purified from bovine milk by affinity chromatography resulted in a decrease in the amount of the high molecular weight form (58,000) with a concomitant increase in the amount of lower molecular weight form (42,000) with little loss of activity. After extensive activity loss, a peptide of molecular weight 38,000 remained as the predominant species and ...
متن کاملStructure of bovine β-lactoglobulin-lactoferrin coacervates.
Lactoferrin (LF) and β-lactoglobulin (BLG) are among the protein pairs that exhibit heteroprotein coacervation, a unique and relatively unexamined type of liquid-liquid phase separation (LLPS). In prior work we found that LF and BLG undergo coacervation at highly constrained conditions of pH, ionic strength and protein stoichiometry. The molar stoichiometry in coacervate and supernatant is LF :...
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BACKGROUND Lactoferrin (LF), a member of the transferrin family, recently has been demonstrated to have anticancer effects on various cancers including oral squamous cell carcinoma (OSCC). However, little is known about the underlying mechanisms of its effects on OSCC. Therefore, we aimed to investigate the mechanism of the suppressive effects of bovine LF (bLF) on the growth of OSCC cells. M...
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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 Dairy Science
سال: 1989
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(89)79215-8