Results 131 to 140 of about 18,290 (187)

Heterogeneity of ceruloplasmin

Clinica Chimica Acta, 1962
Abstract 1. (1) The heterogeneity of serum ceruloplasmin was studied by starch gel electro-phoresis, immuno-electrophoresis and ultracentrifugal techniques. 2. (2) All the preparations of ceruloplasmin, prepared by larger scale methods, were found to consist of multiple components with the characteristics of ceruloplasmin.
M D, POULIK, A G, BEARN
openaire   +2 more sources

Dolphin ceruloplasmin: The first proteolytically stable mammalian ceruloplasmin

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1992
1. Ceruloplasmin, the blue protein of the plasma of vertebrates, was isolated from dolphin, a marine mammal. The protein showed overall physico-chemical parameters very similar to those of all other mammalian ceruloplasmins. The spectroscopic properties indicated a conservation of the copper binding sites. 2.
M. C. Bonaccorsi di Patti, GALTIERI, Antonio, A. Giartosio, G. Musci, L. Calabrese   +4 more
openaire   +4 more sources

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 ...
M, Herve, A, Garnier-Suillerot, L, Tosi, M, Steinbuch   +3 more
openaire   +2 more sources

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, Manolis, D W, Cox
openaire   +2 more sources

Heterogeneity of Human Ceruloplasmin

Science, 1960
Subfractionation of purified human ceruloplasmin, prepared from plasma of 9109 donors, has been carried out by chromatography on columns of diethylaminoethyl cellulose and hydroxylapatite. Electrophoretic analyses of these subfractions on starch gels, at p H 8.5 and 5.7, reveal the presence of at least four ...
A G, MORELL, I H, SCHEINBERG
openaire   +2 more sources

Ceruloplasmin and cardiovascular disease

Free Radical Biology and Medicine, 2000
Transition metal ion-mediated oxidation is a commonly used model system for studies of the chemical, structural, and functional modifications of low-density lipoprotein (LDL). The physiological relevance of studies using free metal ions is unclear and has led to an exploration of free metal ion-independent mechanisms of oxidation.
P L, Fox, B, Mazumder, E, Ehrenwald, C K, Mukhopadhyay   +3 more
openaire   +2 more sources

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, I M, Vasiletz, M M, Shavlovsky   +2 more
openaire   +2 more sources

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
Andrey V. Vasin, Natalia A. Platonova, R.G. Povalihin, Sergey A. Klotchenko, Sergey Samsonov, Nadezhda V. Tsymbalenko, Ludmila V. Puchkova   +6 more
openaire   +2 more sources

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.
E T, Zakharova, M M, Shavlovski, M G, Bass, A A, Gridasova, M O, Pulina, V, De Filippis, M, Beltramini, P, Di Muro, B, Salvato, A, Fontana, V B, Vasilyev, V S, Gaitskhoki   +11 more
openaire   +2 more sources

Ceruloplasmin in neurodegenerative diseases

Brain Research Reviews, 2005
For decades, abnormalities in ceruloplasmin (Cp) synthesis have been associated with neurodegenerative disease. From the early observation that low circulating serum ceruloplasmin levels served as a marker for Wilson's disease to the recent characterization of a neurodegenerative disorder associated with a complete lack of serum ceruloplasmin, the link
Vassiliev V, Harris ZL, Zatta P.
openaire   +3 more sources