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Preparative biochemistry.

Discontinued
Periodical
Biochemistry
Publisher:
Dekker.. New York Ny : Marcel Dekker
Frequency: Four no. a year
Country: United States
Language: English
Start Year:1971 - 1995
Identifiers
ISSN:0032-7484 (Print)
0032-7484 (Linking)
NLM ID:1276634
(DNLM):P23440000(s)
(OCoLC):01589130
Coden:PRBCBQ
Classification:W1 PR424
Purification of brush border membrane vesicles from horse kidney cortex using Percoll.
Preparative biochemistry    January 1, 1988   Volume 18, Issue 1 1-15 doi: 10.1080/00327488808062510
Boudouard M, Giudicelli J, Sudaka P.A rapid method for preparation of brush border membrane vesicles from a large amount of horse kidney cortex is described. Self-orienting Percoll-gradient centrifugation minimized contamination by microsomal membranes. The characteristics of this preparation were checked by electron microscopy and measurement of L-alanine uptake.
Horse plasma ceruloplasmin molecular weight and subunit analysis.
Preparative biochemistry    January 1, 1987   Volume 17, Issue 4 447-454 doi: 10.1080/00327488708062507
Medda R, Cara N, Floris G.Ceruloplasmin is a blue copper-containing serum glycoprotein with oxidase activity. It as been proposed that the physiological function of ceruloplasmin involves the oxidation of ferrous iron and its incorporation into apotransferrin. There are several reports demonstrating that ceruloplasmin is made up of multiple chains. Ryden has questioned the multichain structure of ceruloplasmin from human, pig, horse and rabbit sera, arguing that the dissociation observed by previous workers could be attributed to cleavage of labile bands in the protein by enzymatic contaminants present in commercial pr...
Purification, characterization, and quantitation of the antigen employed in the immunodiffusion test for diagnosis of equine infectious anemia.
Preparative biochemistry    January 1, 1976   Volume 6, Issue 2-3 193-211 doi: 10.1080/00327487608061612
Hart LT, Braymer HD, Larson AD, Broussard EA.Equine infectious anemia (EIA) antigen extracted from the spleen of horses infected with EIA virus was purified by pH treatment, (NH4)2SO4 fractionation and affinity chromatography. The homogeneity of the antigen was indicated by sedimentation rate and sedimentation equilibrium experiments. A S20,w of 0.51 was determined and a molecular weight of 7600 was calculated from sedimentation equilibrium analysis. The amino acid composition of the pure antigen indicated the antigen is an acidic protein. Employing radical immunodiffusion (RID) and pure antigen a method for quantitating antigen content ...