Results 281 to 290 of about 2,131,700 (307)
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Purification of the interferons

Pharmacology & Therapeutics, 1985
Many procedures have been described for the partial purification of human and animal interferons (for review and additional citations, see Berg, 1982; Pestka, 1981a, b, 1983). Although partial purification and purification of the interferons as bands on SDSpolyacrylamide gels was reported by a number of groups, it was not until 1978 and thereafter that
S, Pestka, S J, Tarnowski
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Purification of allergens

Current Opinion in Immunology, 1988
Inhaled allergens derived from pollens, dust mites, animal danders, insects and fungi, are the most common cause of immunoglobulin (Ig) E antibody responses in developed countries. Purilication of allergens from these vanous sources is essential for structural and immunological studies investigating why these molecules readily induce IgE antibody ...
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Purification of Fibronectin

Current Protocols in Cell Biology, 1999
AbstractThis unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium. Fibronectin can be used in cell adhesion and migration assays, and can be obtained in relatively high purity using simple affinity chromatography techniques ...
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Purification of Pancreozymin

Gastroenterology, 1963
Summary The methods of molecular sieving through gel filtration on Sephadex G-50 (fine grade) and ion exchange chromatography on TEAE and DEAE cellulose and CMC were used for the purification of pancreozymin from concentrates of hog small intestine. A purification of at least 30-fold over the starting material could be obtained in two steps.
A P, DHARIWAL   +5 more
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THE PURIFICATION OF HAPTOGLOBIN

Canadian Journal of Biochemistry and Physiology, 1961
A 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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Purification of rennin

Journal of Dairy Research, 1971
SummaryA method based on salt fractionation, iso-electric precipitation and gel filtration chromatography is described for the purification of the enzyme rennin (E.C. 3.4.4.3).
A V, Castle, J V, Wheelock
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Purification of amyloglucosidase

Analytical Biochemistry, 1983
Amyloglucosidase (glucoamylase; EC 3.2.1.3) has been purified from the culture filtrates of Aspergillus candidus Link var. aureus using hydrophobic interaction chromatography and DEAE-cellulose treatment. The enzyme thus obtained has a specific activity of 329 units/mg protein with the overall recoveries between 70 and 75%. The process appears to be of
P B, Mahajan, S R, Kolhekar, P S, Borkar
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Purification of chaperonins

Journal of Chromatography B: Biomedical Sciences and Applications, 1999
The availability of protein samples of sufficient quality and in sufficient quantity is a driving force in biology and biotechnology. Protein samples that are free of critical contaminants are required for specific assays. Large amounts of highly homogeneous and reproducible material are needed for crystallography and nuclear magnetic resonance studies
E, Quaite-Randall, A, Joachimiak
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Purification of microcystins

Journal of Chromatography A, 2001
Microcystins are an increasingly important group of bioactive compounds produced by a number of mainly planktonic cyanobacteria. They are a family of cyclic heptapeptides that cause both acute and chronic toxicity. Purified microcystins are utilised in a range of research applications including toxicological and biochemical studies, development of ...
L A, Lawton, C, Edwards
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Purification of Vitronectin

Current Protocols in Cell Biology, 1999
AbstractThis unit describes the purification of extracellular vitronectin from plasma by a series of affinity chromatography steps. First plasma is depleted of fibronectin and other heparin‐binding proteins; the sample is then treated with urea to activate the heparin‐binding activity of vitronectin. The resulting vitronectin is ∼98% pure.
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