Microcalorimetry in Biochemical Analysis

Martin, C. Dianne; Marini, Mario; Brown, Harry

doi:10.1080/10408347908542712

Cited by 13 publications

(10 citation statements)

References 125 publications

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“…Наиболее свежая публикация на данную тему говорит об использовании схемы DEBIRI парал-лельно с режимом mFOLFOX6 и mFOLFOX6 с бева-цизумабом. По данным исследования, у пациентов группы DEBIRI чаще отмечался объективный ответ на лечение через 2 мес (78 % против 54 %; p = 0,02), 4 мес (95 % против 70 %; p = 0,03), 6 мес (76 % против 60 %; p = 0,05), а также более длительная медиана выживае-мости без прогрессирования (15,3 мес против 7,6 мес) [38]. В табл.…”

Section: особенности метаболизмаunclassified

Irinotecan in the treatment of colorectal cancer. A literature review

Иванов¹,

Гордеев²,

Байчоров³

et al. 2017

Onkol. koloproktol.

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Section: особенности метаболизмаunclassified

Irinotecan in the treatment of colorectal cancer. A literature review

Иванов¹,

Гордеев²,

Байчоров³

et al. 2017

Onkol. koloproktol.

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“…When crystallographic structures of antigenantibody complexes are not available, the conformation of combining site loops can be predicted starting from known structures presenting highly homologous sequences (Chothia and Lesk, 1987;Chothia et al, 1989). Energy minimization and molecular dynamics studies can be used to find low energy conformations (Bruccoleri et al, 1988;Fine et al, 1986;Martin et al, 1989;Smith-Gill et al, 1987). NMR analysis of intermolecular nuclear Overhauser effects can provide information on the distance between antigen and antibody atoms and restraints on interproton distances can be used to dock the antigen into the antibody combining site (Scherf et al, 1992;Zilber et al, 1990).…”

Section: Usefulness Of Quantitative Measurementsmentioning

confidence: 99%

Epitope analysis using kinetic measurements of antibody binding to synthetic peptides presenting single amino acid substitutions

Zeder‐Lutz

Altschuh

Denery-Papini

et al. 1993

J of Molecular Recognition

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The fine modulation of peptide-antibody interactions was investigated with anti-peptide monoclonal antibodies recognizing peptide 125-136 of the coat protein of tobacco mosaic virus. Nine synthetic peptides presenting single amino acid substitutions were selected for detailed analysis on the basis of their reactivity in ELISA. Kinetic measurements of the binding of four antibodies to these peptides performed with a biosensor instrument (BIAcore, Pharmacia) were used to quantify the contribution of individual residues to antibody binding. The results showed that even conservative exchanges of some residues in the epitope resulted in a small but significant decrease of the equilibrium affinity constant due mostly to a higher dissociation rate constant of the monoclonal antibodies. Two amino acid residues directly adjacent to the epitope, which appeared to play no role when tested by ELISA, were shown to influence the kinetics of binding. These data should be useful for computer modelling of the peptide-antibody interactions.

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“…Experimental evaluation of the rate constants and a solution of the requisite differential equations can lead to a reconstruction of the "adiabatic" heat curve. 20,21 For the titration of HC1, correction need not be made for volume changes, since only 4 pl are added to the 2.0-ml volume. Thermal titration curves of proteins, however, require not only volume change corrections, but also corrections for the contribution to Qobs by free acidity in addition to their correction to the "adiabatic" state.…”

Section: Data Treatmentmentioning

confidence: 99%

Calorimetric determination of the enthalpy of ionization of oxidized and reduced horse heart cytochrome c

1980

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SynopsisThe heats of ionization of protons, AH,, of oxidized and reduced horse heart cytochrome c in 0.15M KC1 a t 20°C were determined using a titration calorimeter which simultaneously afforded the potentiometric titration curve. Reproducibility of the thermal titrations is within 2%, and evaluation of the heats observed after the heat loss corrections is estimated to be within 5%. A single titration of oxidized cytochrome c from pH 11 to 3 is in excellent agreement with the thermal titration of this protein obtained with flow calorimetry. The thermal titration, however, is not reversible, due in part to the loss of titratable group(s) in this pH region and to the heat contribution of the acid and alkaline conformational changes which occur. Although of lesser magnitude, the reduced form also indicates similar thermal transitions. These differences are due solely to conformational contributions to the thermal process, since the potentiometric curves are reversible. The nature of the irreversibility for oxidized cytochrome c appears to involve the loss of a group with pK' 8.9 and the shift of two groups from pK' 5.6 to 4.8. Thermal difference curves for this process indicate that heats of -7.8 and -24.1 kcal/mol are liberated which are centered at pH 9.3 and 3.9, respectively.

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Microcalorimetry in Biochemical Analysis

Cited by 13 publications

References 125 publications

Irinotecan in the treatment of colorectal cancer. A literature review

Irinotecan in the treatment of colorectal cancer. A literature review

Epitope analysis using kinetic measurements of antibody binding to synthetic peptides presenting single amino acid substitutions

Calorimetric determination of the enthalpy of ionization of oxidized and reduced horse heart cytochrome c

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