Results 231 to 240 of about 35,641 (262)

Interaction of Lactoferrin with Ceruloplasmin

Archives of Biochemistry and Biophysics, 2000
When added to human blood serum, the iron-binding protein lactoferrin (LF) purified from breast milk interacts with ceruloplasmin (CP), a copper-containing oxidase. Selective binding of LF to CP is evidenced by the results of polyacrylamide gel electrophoresis, immunodiffusion, gel filtration, and affinity chromatography.
Paolo Di Muro, E. T. Zakharova, Anastasia A. Gridasova, Mikhail G. Bass, M. O. Pulina, Benedetto Salvato, Mikhail M. Shavlovski, Vincenzo De Filippis, Vladimir S. Gaitskhoki, Mariano Beltramini, Angelo Fontana, Vadim B. Vasilyev   +11 more
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Reaction of human ceruloplasmin and anion treated ceruloplasmin with diethyldithiocarbamate

Journal of Inorganic Biochemistry, 1985
The reaction of human ceruloplasmin and anion treated ceruloplasmin with diethyldithiocarbamate was studied at pH 5.5. The analysis of optical and EPR spectra at 9 GHz showed that ceruloplasmin contains five paramagnetic copper ions, two of which, X and Y, not involved in enzymatic activity, are chelated by diethyldithiocarbamate; the complex thus ...
Arlette Garnier-Suillerot, Lucia Tosi, Marion Steinbuch, Martine Herve   +3 more
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Molecular pathology of ceruloplasmin

Biochemical Genetics, 1972
Individual preparations of CP isolated from one normal donor and two homozygotes for the “Wilson's disease gene” were subjected to a comparative structural and analytical examination. Analysis of CP tryptic hydrolysate by the peptide map technique revealed 64–66 peptides in each sample.
S. A. Neifakh, M. M. Shavlovsky, I. M. Vasiletz   +2 more
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Mitochondrial ceruloplasmin of mammals

Molecular Biology, 2005
Using immunoblotting method it was found out that ceruloplasmin (Cp) polypeptides are revealed in mitochondria of rats, isolated from brain, liver, testicles and mammary gland. Cp is localized in matrix and inner membranes of mitochondria. Its molecular weight corresponds to the non-glycosilated form of the protein. Computer analysis did not reveal any
N. V. Tsymbalenko, Andrey V. Vasin, R. G. Povalikhin, N. A. Platonova, L. V. Puchkova, S A Samsonov, S. A. Klotchenko   +6 more
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Ceruloplasmin in neurodegenerative diseases

Biochemical Society Transactions, 2008
Two decades ago, patients lacking circulating serum ceruloplasmin (Cp) presented with neurodegeneration associated with brain iron accumulation. These patients, with mutations in the MCO (multi-copper oxidase), Cp, revealed an essential role for Cp in iron homoeostasis.
Sarah J. Texel, Z. Leah Harris, Xueying Xu   +2 more
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On the conformation of porcine ceruloplasmin

Archives of Biochemistry and Biophysics, 1969
Abstract The ultracentrifugal behavior and optical properties of porcine ceruloplasmin have been measured to elucidate the conformation of the protein molecule. The molecular weights of apo- and reduced porcine ceruloplasmin are almost identical with that of native protein, i.e., about 150,000, whereas their sedimentation velocities are slightly ...
Yozo Hibino, Yoshiaki Nosoh, Tatsuya Samejima, Shozo Kajiyama   +3 more
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Purification of Rat Ceruloplasmin: Characterization and Comparison with Human Ceruloplasmin

Preparative Biochemistry, 1980
Rat ceruloplasmin was purified by a three-step column chromatography procedure, utilizing DEAE-Sepharose, Sepharose CL-6B, and CM-Sephadex A50 columns. The molecular weight of rat ceruloplasmin determined by a molecular sieve column was 124,000 daltons.
A. Manolls, D. W. Cox
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Sheep ceruloplasmin: isolation and characterization [PDF]

Molecular and Cellular Biochemistry, 1983
Ceruloplasmin has been isolated from sheep plasma by a procedure involving two chromatographic steps and (NH4)2SO4 fractionation. The ovine protein is similar to ceruloplasmins from other species previously described (human, bovine), having a single chain of about 125 Kdal with a very high degree of homology in the amino acid composition.
Antonio Galtieri, Capuozzo E, Ersilia Bellocco, Calabrese L, Calabrese L   +4 more
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Ceruloplasmin receptors of erythrocytes

Biochemical and Biophysical Research Communications, 1984
Mammalian erythrocytes have been shown to bind 125I labeled ceruloplasmin. Binding was reversible and specific. Scatchard analysis yielded linear plots with a Kd of approximately 5nM. The binding site appeared to be a protein located on the cell surface.
Earl Frieden, Grady Barnes
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Interaction of ceruloplasmin, lactoferrin, and myeloperoxidase [PDF]

Biochemistry (Moscow), 2007
When lactoferrin (LF) and myeloperoxidase (MPO) are added to ceruloplasmin (CP), a CP-LF-MPO triple complex forms. The complex is formed under physiological conditions, but also in the course of SDS-free PAGE. Polyclonal antibodies to both LF and MPO displace the respective proteins from the CP-LF-MPO complex.
Alexander G. Markov, E. T. Zakharova, N. I. Kolodkin, Vadim B. Vasilyev, M. N. Berlov, M. O. Pulina, M. I. Ayrapetov, Piotr Yablonsky, K. V. Ageeva, George N. Volgin, Alexey V. Sokolov   +10 more
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