BIOMAT Database Logo BIOMAT Database Logo

Iron-binding fragments from the N-terminal and C-terminal regions of human lactoferrin. 1978

J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson

Digestion of lactoferrin with pepsin at pH3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%-iron-saturated lactoferrin yielded the N- and C-terminal half molecules, which could be separated by DEAE-Sephadex chromatography. The N- and C-terminal fragments did not show any immunological cross-reaction. The carbohydrate of lactoferrin was distributed equally between the two fragments.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D007781 Lactoferrin An iron-binding protein that was originally characterized as a milk protein. It is widely distributed in secretory fluids and is found in the neutrophilic granules of LEUKOCYTES. The N-terminal part of lactoferrin possesses a serine protease which functions to inactivate the TYPE III SECRETION SYSTEM used by bacteria to export virulence proteins for host cell invasion. Lactotransferrin
D007782 Lactoglobulins Globulins of milk obtained from the WHEY. Lactoglobulin,beta-Lactoglobulin,beta-Lactoglobulin A,beta-Lactoglobulin B,beta-Lactoglobulin C,beta-Lactoglobulin E,beta-Lactoglobulin F,beta-Lactoglobulin G,beta-Lactoglobulin I,beta Lactoglobulin,beta Lactoglobulin A,beta Lactoglobulin B,beta Lactoglobulin C,beta Lactoglobulin E,beta Lactoglobulin F,beta Lactoglobulin G,beta Lactoglobulin I
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002241 Carbohydrates A class of organic compounds composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n. The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES. Carbohydrate
D002621 Chemistry A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Studies of the binding of different iron donors to human serum transferrin and isolation of iron-binding fragments from the N- and C-terminal regions of the protein.
August 1978, The Biochemical journal,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
The preparation and partial characterization of N-terminal and C-terminal iron-binding fragments from rabbit serum transferrin.
September 1982, The Biochemical journal,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Regions located in both the N-lobe and C-lobe of human lactoferrin participate in the binding interaction with bacterial lactoferrin receptors.
May 1993, Microbial pathogenesis,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Iron-binding fragments from the carboxyl-terminal region of hen ovotransferrin.
July 1975, The Biochemical journal,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
The N-terminal sequence of paratropomyosin binding fragments from beta-connectin.
March 2003, Bioscience, biotechnology, and biochemistry,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Functional roles of the N- and C-terminal regions of the human mitochondrial single-stranded DNA-binding protein.
October 2010, PloS one,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- and C-terminal low affinity contributing regions.
August 2000, FEBS letters,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Crystal structure and iron-binding properties of the R210K mutant of the N-lobe of human lactoferrin: implications for iron release from transferrins.
June 2000, Biochemistry,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme.
January 2009, Biochemistry,
J M Bluard-Deconinck, and J Williams, and R W Evans, and J van Snick, and P A Osinski, and P L Masson
Structural and functional characterization of proteolytic fragments derived from the C-terminal regions of bovine fibrinogen.
May 1995, European journal of biochemistry,
Copied contents to your clipboard!