The Nature of the Cell Surface Receptor Site for Lens culinaris Phytohemagglutinin

Kornfeld, Stuart; Rogers, John C.; Gregory, Walter

doi:10.1016/s0021-9258(19)34153-5

Cited by 123 publications

(15 citation statements)

References 23 publications

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“…The only limit is set by the sensitivity of the fluorometer. In this study it was 10~9 M and is to be compared with 10_l 1 M for radioiodinated lectins (Cuatrecasas, 1973; Kornfeld et al, 1971). However, it must be mentioned that the lower sensitivity in our studies is due to the absorption quenching of the fluorescence by the liberated hemoglobin.…”

Section: Discussionmentioning

confidence: 99%

“…preferred over ,3lI-labeled protein used in a previous study (Kornfeld et al, 1971) because manipulation of fluoresceinated material requires less precautions or facilities than radiolabeled protein and has proved to be very accurate and sensitive for the study of membrane receptors (Schreiber et al, 1978). This paper presents a complete quantitative equilibrium and kinetic analysis of the binding of LL to the erythrocyte receptors.…”

mentioning

confidence: 99%

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Equilibrium and kinetic studies of the binding of Lens culinaris lectin to rabbit erythrocytes by a quantitative fluorometric method

Hoebeke¹,

Foriers²,

Schreiber³

et al. 1978

Biochemistry

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The binding of Lens culinaris lectin to the receptors of rabbit erythrocytes was studied by a quantitative fluorometric method using the fluoresceinated conjugate. Equilibrium data showed the presence of 1.2 x 10(6) receptors/cell with an association constant varying from 8 to 3 x 10(6) M-1 over a temperature range of 5 to 37 degrees C. The binding reaction is exothermic with a deltaH = -4.6 kcal/mol and a deltaS = + 15 eu. It appears that most of the bound lectin molecules had only a single site occupied, the agglutination being due to a very low fraction (0.0003--0.0056) of lectin molecules with two sites occupied. The specificity of the reaction was demonstrated through its inhibition by nonfluoresceinated LL and by the specific sugars methyl alpha-D-glucoside and methyl alpha-D-mannoside. From the inhibition curves an association constant of 4 x 10(2) M-1 was calculated for methyl alpha-d-glucoside and 9 x 10(2) for methyl alpha-D-mannoside. The association and dissociation rate constants of the binding reaction are, respectively, in the range of 3--10 x 103 and 3--33 x 10(-4) M-1 s-1 in the temperature range of 5 to 37 degrees C. The activation energies of the forward and reverse reactions are 7 and 13 kcal/mol, respectively. The association constants and the binding enthalpy calculated from the activation energies were fully consistent with those obtained by equilibrium measurements.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Equilibrium and kinetic studies of the binding of Lens culinaris lectin to rabbit erythrocytes by a quantitative fluorometric method

Hoebeke¹,

Foriers²,

Schreiber³

et al. 1978

Biochemistry

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“…Although the distribution of these glycopeptides among the individual glycoproteins is not known some inferences may now be drawn from the specificities of the two lectins used in the present study. In addition to the requirement for mannose residues, glucosamine also appears to be involved in the binding of glycoproteins to LcH (Kornfeld et al. 1971).…”

Section: Discussionmentioning

confidence: 99%

Fractionation of synaptic plasma membrane glycoproteins by lectin affinity chromatography

Gurd¹,

Mahler²

1974

Biochemistry

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“…Lymphocytes are stimulated to divide in the presence of certain lectins (see review, Ling, 1968). The cell surface receptor sites for several of these lectins have been characterized as glycoproteins (Kornfeld et al, 1971).…”

Section: Discussionmentioning

confidence: 99%

Glycoproteins from the surface of metaphase cells

Glick¹,

Buck²

1973

Biochemistry

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The Nature of the Cell Surface Receptor Site for Lens culinaris Phytohemagglutinin

Cited by 123 publications

References 23 publications

Equilibrium and kinetic studies of the binding of Lens culinaris lectin to rabbit erythrocytes by a quantitative fluorometric method

Equilibrium and kinetic studies of the binding of Lens culinaris lectin to rabbit erythrocytes by a quantitative fluorometric method

Fractionation of synaptic plasma membrane glycoproteins by lectin affinity chromatography

Glycoproteins from the surface of metaphase cells

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