Structured Review

PerkinElmer α 32 p atp radionucleotide
<t>ATP</t> hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.
α 32 P Atp Radionucleotide, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/α 32 p atp radionucleotide/product/PerkinElmer
Average 91 stars, based on 1 article reviews
Price from $9.99 to $1999.99
α 32 p atp radionucleotide - by Bioz Stars, 2020-04
91/100 stars

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1) Product Images from "Negative cooperativity in the nitrogenase Fe protein electron delivery cycle"

Article Title: Negative cooperativity in the nitrogenase Fe protein electron delivery cycle

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1613089113

ATP hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.
Figure Legend Snippet: ATP hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.

Techniques Used: Flow Cytometry, Derivative Assay

Related Articles

Protein Purification:

Article Title: Negative cooperativity in the nitrogenase Fe protein electron delivery cycle
Article Snippet: Paragraph title: Materials, Buffers, Protein Purification, and Activity Assays. ... [α-32 P]ATP radionucleotide was purchased from PerkinElmer.

Activity Assay:

Article Title: Negative cooperativity in the nitrogenase Fe protein electron delivery cycle
Article Snippet: Paragraph title: Materials, Buffers, Protein Purification, and Activity Assays. ... [α-32 P]ATP radionucleotide was purchased from PerkinElmer.

Purification:

Article Title: Negative cooperativity in the nitrogenase Fe protein electron delivery cycle
Article Snippet: [α-32 P]ATP radionucleotide was purchased from PerkinElmer. .. Nitrogenase proteins were expressed and purified from A. vinelandii strains DJ995 (wild-type MoFe protein with His tag) and DJ884 (wild-type Fe protein) as described previously ( ).

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    PerkinElmer α 32 p atp radionucleotide
    <t>ATP</t> hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.
    α 32 P Atp Radionucleotide, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α 32 p atp radionucleotide/product/PerkinElmer
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α 32 p atp radionucleotide - by Bioz Stars, 2020-04
    91/100 stars
      Buy from Supplier

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    ATP hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Negative cooperativity in the nitrogenase Fe protein electron delivery cycle

    doi: 10.1073/pnas.1613089113

    Figure Lengend Snippet: ATP hydrolysis data fits. Presteady-state, quench-flow measurements of the time course of ATP hydrolysis by rapidly mixing MoFe protein (10 μM) and Fe protein (40 μM) with [α- 32 P]ATP (2 mM) (●). Dashed black line: half-sites model, Scheme B, using rate constants, k ET = 140 s −1 , k ATP = 36 s −1 , k Pi = 16 s −1 , and k off = 11.9 s −1 , as derived from the phenomenological fits to the experimental data, along with the recharging model. Solid black line: independent-sites model, Scheme A, calculated analogously. Red line: calculated from the rate parameters obtained by the global fit to negative cooperativity Scheme C, as given in the scheme. ( Inset ) Data and simulations to longer times.

    Article Snippet: [α-32 P]ATP radionucleotide was purchased from PerkinElmer.

    Techniques: Flow Cytometry, Derivative Assay