نتایج جستجو برای: bovine lactoferrin

تعداد نتایج: 76071  

Journal: :Applied and environmental microbiology 1992
F Ascencio A Ljungh T Wadstrom

Various lactoferrin preparations (iron-saturated and iron-depleted human milk lactoferrins and bovine milk and colostrum lactoferrins) were bound by Aeromonas hydrophila. Binding was (i) reversible (65% of bound lactoferrin was displaced by unlabeled lactoferrin), (ii) specific (lactoferrin but not other iron-containing glycoproteins such as ferritin, transferrin, hemoglobin, and myoglobin inhi...

2000
Craig R. Baumrucker

Lactoferrin (Lf) is an iron-binding protein found in high concentrations in mammary secretions but synthesized by many tissues. Bovine mammary tissue secretes μg/ml mass of Lf in milk, but during involution and prepartum periods, 20–80 mg/ml concentrations may be observed. While a number of functions have been ascribed to lactoferrin, only the antimicrobial and lymphocyte interactions have comp...

Journal: :The Journal of nutrition 2010
Yalin Liao Xiaogu Du Bo Lönnerdal

Lactoferrin (Lf) is an abundantly expressed protein in human milk. Lactoferrin exhibits several important biological functions, and its expression is regulated by multiple environmental factors. Cellular endogenous factors, however, have not been extensively studied with regard to lactoferrin gene expression. In this study, we showed that lactoferrin gene expression and function are directly ta...

Journal: :Journal of virology 1997
M Yi S Kaneko D Y Yu S Murakami

Hepatitis C virus (HCV) has two envelope proteins, E1 and E2, which form a heterooligomer. During dissection of interacting regions of HCV E1 and E2, we found the presence of an interfering compound or compounds in skim milk. Here we report that human as well as bovine lactoferrin, a multifunctional immunomodulator, binds two HCV envelope proteins. As determined by far-Western blotting, the bac...

Journal: :Infection and immunity 2002
Takahiko Oho Morihide Mitoma Toshihiko Koga

The bovine lactoferrin molecule and relatively long lactoferrin fragments containing residues 473 to 538 strongly inhibited adherence of Streptococcus mutans to saliva-coated hydroxyapatite beads. Each cysteine residue in Lf411 (residues 473 to 538) was replaced by a serine residue, and the mutants Lf411-C481S and Lf411-C532S strongly inhibited S. mutans adherence. These results suggest that th...

Journal: :Infection and immunity 2001
A Håkansson H Roche S Mirza L S McDaniel A Brooks-Walter D E Briles

Human lactoferrin is an iron-binding glycoprotein that is particularly prominent in exocrine secretions and leukocytes and is also found in serum, especially during inflammation. It is able to sequester iron from microbes and has immunomodulatory functions, including inhibition of both complement activation and cytokine production. This study used mutants lacking pneumococcal surface protein A ...

2017
Fatemeh Amiri Fatemeh Moradian Alireza Rafiei

Corresponding Author: Fatemeh Moradian Assistant professor of Biochemistry, Basic Sciences Group, Sari Agricultural Sciences and Natural Resources University, Sari, Mazandaran, Iran, P.O.B. 578. Telefax:+98-11-33687655 E-mail: [email protected] & [email protected] Abstract Background: Lactoferrin is a glycoprotein with a molecular weight of 80 kDa, as a member of the transferring family. In...

Journal: :Endocrinology 2004
Jillian Cornish Karen E Callon Dorit Naot Kate P Palmano Tatjana Banovic Usha Bava Maureen Watson Jian-Ming Lin P C Tong Qi Chen Vincent A Chan Helen E Reid Nick Fazzalari Heather M Baker Edward N Baker Neill W Haggarty Andrew B Grey Ian R Reid

Lactoferrin is an iron-binding glycoprotein present in epithelial secretions, such as milk, and in the secondary granules of neutrophils. We found it to be present in fractions of milk protein that stimulated osteoblast growth, so we assessed its effects on bone cell function. Lactoferrin produced large, dose-related increases in thymidine incorporation in primary or cell line cultures of human...

Journal: :Glycobiology 1997
M Lopez B Coddeville J Langridge Y Plancke P Sautière H Chaabihi F Chirat A Harduin-Lepers M Cerutti A Verbert P Delannoy

The development of therapeutic glycoprotein production using the baculovirus expression system depends on the ability of insect cell lines to reproduce site specific mammalian-like N-glycans. A combination of 1H-NMR and mass spectrometry techniques (MALD-MS, ES-MS, and CID-MS-MS) allowed us to elucidate the N-linked oligosaccharides microheterogeneity on three different N-glycosylation sites, A...

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