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On the mechanism of the Zn2+ and CO2+-alkaline phosphatases of E. coli. Number of sites and anticooperativity

Biochemical and biophysical research communications, 1969-11, Vol.37 (5), p.744-749

1969

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The Mn2+- alkaline phosphatase of E. coli

Biochemical and biophysical research communications, 1970-07, Vol.40 (1), p.91-96

1970

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The functional properties of the Zn2(plus)-and Co2(plus)-alkaline phosphatases of Escherichia coli. Labelling of the active site with pyrophosphate, complex formation with arsenate, and reinvestigation of the role of the zinc atoms

European journal of biochemistry, 1970-06, Vol.14 (2), p.301-308

1970

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Milk alkaline phosphatase. Stimulation by Mg2+ and properties of the Mg2+ site

Biochimica et Biophysica Acta (BBA) - Enzymology, 1977-07, Vol.483 (1), p.100-106

1977

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Aminopeptidase N from Escherichia coli: Ionizable Active‐Center Groups and Substrate Specificity

European journal of biochemistry, 1977-12, Vol.81 (2), p.299-305

1977

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Flip-flop mechanisms in enzymology. A model: the alkaline phosphatase of Escherichia coli

European journal of biochemistry, 1971-05, Vol.20 (1), p.124-139

1971

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Intestinal alkaline phosphatase. Physical properties and quaternary structure

Biochemistry (Easton), 1974-04, Vol.13 (9), p.1783-1788

1974

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Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity

Biochemistry (Easton), 1974-04, Vol.13 (9), p.1788-1795

1974

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The Mn2plus-alkaline phosphatase of E. coli

Biochemical and biophysical research communications, 1970-07, Vol.40 (1), p.91-96

1970

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The Mn 2+- alkaline phosphatase of E. coli

Biochemical and biophysical research communications, 1970, Vol.40 (1), p.91-96

1970

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On the mechanism of the Zn2+ and Co2+-alkaline phosphatase of E. coli. Number of sites and anticooperativity

Biochemical and biophysical research communications, 1969-11, Vol.37 (5), p.744-749

1969

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On the mechanism of the Zn 2+ and CO 2+-alkaline phosphatases of E. coli. Number of sites and anticooperativity

Biochemical and biophysical research communications, 1969, Vol.37 (5), p.744-749

1969

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The Functional Properties of the Zn2+‐and Co2+‐Alkaline Phosphatases of Escherichia coli

European journal of biochemistry, 1970-06, Vol.14 (2), p.301-308

1970

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Negative cooperativity and half of the sites reactivity. Alkaline phosphatases of Escherichia coli with Zn2+, Co2+, Cd2+, Mn2+, and Cu2+ in the active sites

Biochemistry (Easton), 1974-08, Vol.13 (18), p.3754-3762

1974

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Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli. Reconstitution of the Ca2+--phosphatase from the apoenzyme EPR study of the Mn2+-phosphatase

Biochemical and biophysical research communications, 1970-08, Vol.40 (3), p.589-593

1970

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Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli

Biochemical and biophysical research communications, 1970-08, Vol.40 (3), p.589-593

1970

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Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli: Reconstitution of the Cd 2+-phosphatase from the apoenzyme EPR study of the Mn 2+-phosphatase

Biochemical and biophysical research communications, 1970, Vol.40 (3), p.589-593

1970

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Bovine kidney alkaline phosphatase. Purification, subunit structure, and metalloenzyme properties

The Journal of biological chemistry, 1975-08, Vol.250 (15), p.6040-6045

1975

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The Cu2 plus-alkaline phosphatase of Escherichia coli

European journal of biochemistry, 1970-12, Vol.17 (2), p.239-245

1970

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Les parties prenantes de la gouvernance du système olympique

Management & Organisations du Sport, 2022-07, Vol.Issue 4 | 2022

Chappelet, Jean-Loup

2022

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The stakeholders of the Olympic System

Management et Organisations du Sport, 2022-07, Vol.Issue 4 | 2022 (Reviews)

Chappelet, Jean-Loup

2022

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The non-equivalence of the active sites and the mechanism of a mutationally altered E. coli alkaline phosphatase

Biochemical and biophysical research communications, 1975-03, Vol.63 (2), p.529-534

1975

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Bovine kidney alkaline phosphatase: catalytic properties, subunit interactions in the catalytic process, and mechanism of Mg2+ stimulation

The Journal of biological chemistry, 1974, Vol.250 (15), p.6046-6053

1974

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Bovine kidney alkaline phosphatase: purification, subunit structure, and metalloenzyme properties

The Journal of biological chemistry, 1974, Vol.250 (15), p.6040-6045

1974

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Milk alkaline phosphatase. Stimulation by Mg 2+ and properties of the Mg 2+ site

BBA - Enzymology, 1977, Vol.483 (1), p.100-106

1977

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On the mechanism of the Zn2+ and CO2+-alkaline phosphatases of E. coli. Number of sites and anticooperativity

The Mn2+- alkaline phosphatase of E. coli

The functional properties of the Zn2(plus)-and Co2(plus)-alkaline phosphatases of Escherichia coli. Labelling of the active site with pyrophosphate, complex formation with arsenate, and reinvestigation of the role of the zinc atoms

Milk alkaline phosphatase. Stimulation by Mg2+ and properties of the Mg2+ site

Aminopeptidase N from Escherichia coli: Ionizable Active‐Center Groups and Substrate Specificity

Flip-flop mechanisms in enzymology. A model: the alkaline phosphatase of Escherichia coli

Intestinal alkaline phosphatase. Physical properties and quaternary structure

Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivity

The Mn2plus-alkaline phosphatase of E. coli

The Mn 2+- alkaline phosphatase of E. coli

On the mechanism of the Zn2+ and Co2+-alkaline phosphatase of E. coli. Number of sites and anticooperativity

On the mechanism of the Zn 2+ and CO 2+-alkaline phosphatases of E. coli. Number of sites and anticooperativity

The Functional Properties of the Zn2+‐and Co2+‐Alkaline Phosphatases of Escherichia coli

Negative cooperativity and half of the sites reactivity. Alkaline phosphatases of Escherichia coli with Zn2+, Co2+, Cd2+, Mn2+, and Cu2+ in the active sites

Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli. Reconstitution of the Ca2+--phosphatase from the apoenzyme EPR study of the Mn2+-phosphatase

Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli

Tight and loose metal binding sites in the apoalkaline phosphatase of E. coli: Reconstitution of the Cd 2+-phosphatase from the apoenzyme EPR study of the Mn 2+-phosphatase

Bovine kidney alkaline phosphatase. Purification, subunit structure, and metalloenzyme properties

The Cu2 plus-alkaline phosphatase of Escherichia coli

Les parties prenantes de la gouvernance du système olympique

The stakeholders of the Olympic System

The non-equivalence of the active sites and the mechanism of a mutationally altered E. coli alkaline phosphatase

Bovine kidney alkaline phosphatase: catalytic properties, subunit interactions in the catalytic process, and mechanism of Mg2+ stimulation

Bovine kidney alkaline phosphatase: purification, subunit structure, and metalloenzyme properties

Milk alkaline phosphatase. Stimulation by Mg 2+ and properties of the Mg 2+ site

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