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Microheterogeneity of mammalian haptoglobins in isoelectric focusing.
Metadata
JournalComp. Biochem. Physiol., BNot FoundDate
1979
Type
Research Support, U.S. Gov't, P.H.S.
Research Support, Non-U.S. Gov't
Journal Article
Comparative Study
Volume
1979 / 62 : 111-3
Author
Dobryszycka W 1, Krawczyk E
Affiliation

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Doi
PMIDMESH
Animals
Electrophoresis, Polyacrylamide Gel
Haptoglobins
Horses
Humans
Hydrogen-Ion Concentration
Immunodiffusion
Isoelectric Focusing
N-Acetylneuraminic Acid
Peroxidase
Sialic Acids
Swine
Abstract
1. Human haptoglobin type 1-1, porcine haptoglobin, and equine haptoglobin were isolated and purified. 2. These haptoglobins were similar in polyacrylamide gel electrophoresis and in subunit structure but showed microheterogeneity in isoelectric focusing. 3. Isoelectric points of human haptoglobin as determined with photopolymerized gels were found to be 4.03-4.24, of porcine haptoglobin 4.0-4.30, and of horse haptoglobin 3.80-4.15, respectively. 4. Results obtained with chemically polymerized gels were 0.08-0.3 pH units higher. 5. Examined haptoglobins differed also in the ability of complex formation with hemoglobin, in sialic acid content and in antigenic specificity.
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Comp. Biochem. Physiol., BComparative biochemistry and physiology. B, Comparative biochemistry
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