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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
01/08/1992 |
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Data da última atualização: |
12/04/2024 |
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Autoria: |
ZGLICZYNSKI, J. M.; SELVARAJ, R. J.; PAUL, B. B.; STELMASZYWSKA, T.; POSKITT, P. K. F.; SBARRA, A. J. |
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Título: |
Chlorination by the mycloperoxidase-H2O2-Cl-antimicrobial system at acid and neutral pH. |
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Ano de publicação: |
1977 |
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Fonte/Imprenta: |
Proceedings Society Experimental Biology Medical, v. 154, n. 3, p. 418-422, 1977. |
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DOI: |
https://doi.org/10.3181/00379727-154-39 |
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Idioma: |
Inglês |
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Conteúdo: |
The oxidation of Cl- ion by H2O2 yielding Cl+ is catalyzed by myelope-roxidase (MPO) prepared from human PMN. Both H2O2 and CI- in this reaction serve as substrates. Affinity (apparent) studies between MPO and CI- and MPO and H2O2 were carried out. Both (apparent) affinities vary according to pH. The higher the pH, the less the affinity for Cl-. In contrast, the affinity between MPO and H2O2 increases with pH. The dissociation constant of the MPO-CI- enzyme substrate complex is affected by the second substrate, H2O2. The effect of H2O2 on the MPO-C1- affinity is competitive. Likewise, the MPO-H2O2 affinity is decreased with increasing Cl- concentration. This influence is also competitive. From these interactions, it may be concluded that the optimal pH for chlori-nation is dependent on the [H2O2]/[C1-] ratio. The relationship of pH, H2O2, and CI- concentrations may be expressed by the following formula: pH = log [CI-] x560/ [H2O2]. Using the formula, it can be shown that optimal chlorination may occur between pH 4.0 and 7.4. We wish to thank Paul Wallace and Gerry Heatley for technical assistance, Roberta Lemon for preparing the manuscript, and George Daynes for photography. This investigation was supported by Grant CA-1567 awarded by the National Cancer Institute, DHEW, and USPHS Grant HD-1805, NIH. |
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Thesagro: |
Imunologia; Microbiologia. |
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Thesaurus Nal: |
Immunology; Microbiology. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 02051naa a2200241 a 4500
001 1521759
005 2024-04-12
008 1977 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.3181/00379727-154-39$2DOI
100 1 $aZGLICZYNSKI, J. M.
245 $aChlorination by the mycloperoxidase-H2O2-Cl-antimicrobial system at acid and neutral pH.
260 $c1977
520 $aThe oxidation of Cl- ion by H2O2 yielding Cl+ is catalyzed by myelope-roxidase (MPO) prepared from human PMN. Both H2O2 and CI- in this reaction serve as substrates. Affinity (apparent) studies between MPO and CI- and MPO and H2O2 were carried out. Both (apparent) affinities vary according to pH. The higher the pH, the less the affinity for Cl-. In contrast, the affinity between MPO and H2O2 increases with pH. The dissociation constant of the MPO-CI- enzyme substrate complex is affected by the second substrate, H2O2. The effect of H2O2 on the MPO-C1- affinity is competitive. Likewise, the MPO-H2O2 affinity is decreased with increasing Cl- concentration. This influence is also competitive. From these interactions, it may be concluded that the optimal pH for chlori-nation is dependent on the [H2O2]/[C1-] ratio. The relationship of pH, H2O2, and CI- concentrations may be expressed by the following formula: pH = log [CI-] x560/ [H2O2]. Using the formula, it can be shown that optimal chlorination may occur between pH 4.0 and 7.4. We wish to thank Paul Wallace and Gerry Heatley for technical assistance, Roberta Lemon for preparing the manuscript, and George Daynes for photography. This investigation was supported by Grant CA-1567 awarded by the National Cancer Institute, DHEW, and USPHS Grant HD-1805, NIH.
650 $aImmunology
650 $aMicrobiology
650 $aImunologia
650 $aMicrobiologia
700 1 $aSELVARAJ, R. J.
700 1 $aPAUL, B. B.
700 1 $aSTELMASZYWSKA, T.
700 1 $aPOSKITT, P. K. F.
700 1 $aSBARRA, A. J.
773 $tProceedings Society Experimental Biology Medical$gv. 154, n. 3, p. 418-422, 1977.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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