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THE PURIFICATION OF HAPTOGLOBIN
Canadian Journal of Biochemistry and Physiology, 1961A method for preparing haptoglobin in highly purified form from human serum is described. The serum is acidified to pH 4.6 and deionized by gel filtration. Under these conditions haptoglobin is selectively adsorbed from serum by diethyl-aminoethyl-cellulose.
G. E. Connell, R. W. Shaw
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Developmental Medicine & Child Neurology, 1959
SUMMARYHaptoglobins are α2 globulins having the property of combining with haemoglobin. Three main types, controlled by a single pair of genes, are present in all human populations so far tested, and three variant forms have been described. In addition, some individuals have been found in whose sera no haptoglobins could be detected.
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SUMMARYHaptoglobins are α2 globulins having the property of combining with haemoglobin. Three main types, controlled by a single pair of genes, are present in all human populations so far tested, and three variant forms have been described. In addition, some individuals have been found in whose sera no haptoglobins could be detected.
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Haptoglobin Typing of Bloodstains: Electrophoresis of Immunoprecipitated Haptoglobin
Journal of the Forensic Science Society, 1978Haptoglobin has been isolated from free hemoglobin in bloodstain extracts by immuno-precipitation with monospecific antisera. The haptoglobin thus isolated can be typed by electrophoresis on polyacrylamide gels containing the ionic detergent, sodium dodecyl sulfate. Using this method, haptoglobin has been typed in bloodstains up to 18 months of age.
George F. Sensabaugh, E.T. Blake
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Canine haptoglobin: A unique haptoglobin subunit arrangement
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19791. Isolated canine haptoglobin behaved identically to the alpha 2 beta 2 structure typical of human haptoglobin type 1-1 on alkaline polyacrylamide gel electrophoresis and on gel filtration. 2. In the presence of urea or sodium dodecyl sulphate canine haptoglobin dissociated into alpha beta subunits that separated into alpha and beta chains after ...
Barbara H. Bowman +2 more
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Haptoglobin und erythrokinetik
Clinica Chimica Acta, 1959Zusammenfassung Die Plasmahaptoglobine werden bei intravasaler Hamolyse aus dem Kreislauf eliminiert. Der langsame Wiederanstieg der Plasmahaptoglobine nach experimenteller Elimination durch intravenose Hamoglobinzufuhr deutet entweder eine langsame Haptoglobin-Neubildung oder einen schnellen Haptoglobin-Abbau an.
B Nosslin, Nyman Margarrta, K Gydell
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1976
Abstract 1. 1. Plasma from 24 species and subspecies of snakes were examined by starch gel electrophoresis for the presence of haptoglobin. 2. 2. Haptoglobin was found in 17 species. In the remaining 7, no demonstrable haptoglobin was found. 3. 3. No evidence of intra-specific variation was found. 4. 4.
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Abstract 1. 1. Plasma from 24 species and subspecies of snakes were examined by starch gel electrophoresis for the presence of haptoglobin. 2. 2. Haptoglobin was found in 17 species. In the remaining 7, no demonstrable haptoglobin was found. 3. 3. No evidence of intra-specific variation was found. 4. 4.
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Monoclonal antibody to human haptoglobin reacts with goat haptoglobin
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19911. Monoclonal antibody 2.36.71.41 produced to human haptoglobin forms precipitates with goat haptoglobin in double immunodiffusion and electroimmunodiffusion. 2. Solid-phase immunoenzymatic assay (ELISA) based on the reaction of the monoclonal antibody 2.36.71.41 with goat haptoglobin can be used for quantitative estimation of haptoglobin content in ...
Tadeusz Stefaniak +2 more
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Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy
Journal of Molecular Biology, 1984The human serum protein, haptoglobin, forms a stable, irreversible complex with hemoglobin. Haptoglobin is composed of two H chains, which are connected via two smaller L chains to give a protein of 85,000 Mr. In the complex, each H chain binds an alpha beta dimer of hemoglobin for a total molecular weight of 150,000. The scanning transmission electron
James F. Hainfeld +4 more
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Haptoglobin and Increased Haemolysis
Vox Sanguinis, 1962SummaryAn investigation was carried out as to the relationship between increased baemolysis and the serum haptoglobin level. The haemoglobin binding capacity of the serum was estimated in 64 normal adults, 83 healthy elderly persons, 73 patients suffering from various forms of congenital and acquired haemolytic anaemia, 29 patients with non‐haemolytic ...
H. W. Krijnen +2 more
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Localization of Haptoglobin and ABO
Nature, 1965RECENTLY, P. S. Gerald et al.1 published their observations on haptoglobin (Hp) in a family with a child in which one of the D group chromosomes (13, 14 or 15) was deformed into a ring structure, which implies that part of the chromosomal material of the chromosome is deleted.
L. E. Nijenhuis +2 more
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