Results 251 to 260 of about 75,255 (281)

Inhibitory peptides from concanavalin A

Experientia, 1975
Durch Trypsinverdauung von nativem und denaturiertem Concanavalin A wurde eine Peptidfraktion erhalten, die sowohl die hamagglutinierende als auch die mitogene Wirkung von Concanavalin A hemmt. Die Fraktion zeigte jedoch keine Wirkung auf die Aktivitat von Bohnenagglutinin.
D S, Seidl, A, Palozzo, A, Levy, V, Azavache, M, Jaffé, W G, Jaffé   +5 more
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Temperature effects on the concanavalin A molecule and on concanavalin A binding

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
Abstract Under the same conditions generally used for agglutination tests, the concanavalin A molecule undergoes quarternary structure transitions at different temperatures. The tetrameric form is predominant at 37 °C but it dissociates into dimers as the temperature is lowered.
C, Huet, M, Lonchampt, M, Huet, A, Bernadac   +3 more
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The concanavalin a receptor from human erythrocytes in lipid bilayer membranes. Interaction with concanavalin A and succinyl-concanavalin A

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1983
The concanavalin A receptor from human erythrocyte membranes has been isolated by affinity chromatography using the mild, readily-dialyzable detergent dodecyltrimethylammonium bromide. The purified protein has been reincorporated into large unilamellar phospholipid vesicles using a detergent dialysis technique.
C A, Chicken, F J, Sharom
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Effect of concanavalin A and succinyl concanavalin A on cytomegalovirus replication in fibroblasts

Archives of Virology, 1986
In order to investigate inhibition of viral replication, human embryonic fibroblasts infected with cytomegalovirus (CMV) were treated with 0 to 25 micrograms/ml concanavalin A (Con A) and 0 to 150 micrograms/ml succinylated Con A (S-Con A). Alterations in cellular morphology occurred by day 2 post infection (p.i.) in cultures treated with 10 micrograms/
A, Grail, M, Norval
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Concanavalin A: An Introduction

1975
During the last quarter of the nineteenth century and in the beginning of the twentieth century, bacteriologists were searching for agglutinins which could be used as antibacterial agents. Field and Teague (1907), for example, were working with typhoid agglutinins. Kolmer (1923) was working with various other types of antibacterial agglutinins.
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Insulinomimetic homology of concanavalin A

Medical Hypotheses, 1983
A striking peptide sequence and three dimensional conformational homology between a portion of insulin and the plant lectin concanavalin A is described. This amino acid sequence has been demonstrated to be essential to the bioactivity of the hormone insulin.
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Circular dichroism studies on concanavalin A

Biochemical and Biophysical Research Communications, 1971
Abstract Optical rotatory dispersion and circular dichroism studies on native and demetallized concanavalin A indicate that this protein consists essentially of a mixture of β-form and random coil. The induction of α-helix in the native protein is accomplished through the use of 2-chloroethanol. The sequential addition of transition metal, Ca2+ and α-
W D, McCubbin, K, Oikawa, C M, Kay
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A Co(III) derivative of concanavalin A

Biochemical and Biophysical Research Communications, 1979
Abstract Co(III) has been stoichiometrically incorporated into jack bean concanavalin A. The Co(III) protein still possesses a binding site for an additional divalent transition metal ion which together with Ca(II) can induce the sugar binding ability. No H2O2 oxidation of Co(II) occurs with demetallized concanavalin A activated with Ca(II) and Co(II)
M S, Urdea, D J, Christie, G R, Munske, J A, Magnuson, J I, Legg   +4 more
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Cross-linked derivatives of Concanavalin A

1987
Publisher Summary This chapter describes methods for the preparation of covalently cross-linked mono-, di-, and tetravalent Concanavalin A derivatives, which do not undergo subunit exchange. Concanavalin A (Con A) is the most widely used lectin in immunology and cell biology. It activates T lymphocytes, leading to cell division, lymphokine production,
T, Osawa, M, Beppu
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Allergenicity of Concanavalin A in Mice

International Archives of Allergy and Immunology, 1979
Concanavalin A (Con A) is a potent allergen in certain strains of mice and in particularly the H-2K^k mice, A/J, CBA/H, and C3H/He. Using a dose of 100 <i>μ</i>g, the subcutaneous route of injection was the most effective means of inducing high, persistent titers of T cell-dependent circulating anti-Con A reagins ...
G F, Mitchell, A E, Clarke
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