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Lactoperoxidase

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{{#if: | {{#if: | {{#if:6678| {{#if: 612 aa | {{#if: | {{#if: Ca2+, Häm b | {{#if: (712 aa) | {{#if: | {{#if: LPOP220791502051923363 | {{#if: LPO | {{#if: P220791502051923363 | {{#if: | {{#if:| {{#if: | {{#if: 1.11.1.7OxidoreduktaseRedoxreaktionIodid, Bromid, Thiocyanat + H2O2Hypoiodit, Hypobromit, Hypothiocyanit + H2O | {{#if: 1.11.1.7Oxidoreduktase| {{#if: | {{#if: | {{#if: Redoxreaktion| {{#if: Iodid, Bromid, Thiocyanat + H2O2| {{#if: Hypoiodit, Hypobromit, Hypothiocyanit + H2O| {{#if: Tiere{{#if: P22079 | {{#ifeq: | NV ||1}}|}}| {{#if: P22079 | {{#ifeq: | NV || | style="background:#C3FDB8; color:#000000;" | Homologie-Familie {{#if: Tiere | | style="background:#C3FDB8; color:#000000;" | Übergeordnetes Taxon {{#if: | | style="background:#C3FDB8; color:#000000;" | Ausnahmen {{#if: {{#if: Hausmaus | | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe {{#if: ENSG00000167419ENSMUSG00000009356
{{#if: Lactoperoxidase | Lactoperoxidase | Lactoperoxidase }}
Lactoperoxidase }}
Bändermodell der Lactoperoxidase der Hausziege (Capra hircus). Das Protein ist in Regenbogenfarben dargestellt (N-Terminus = blau, C-Terminus = rot) während das Häm mit Kugeln dargestellt ist (Kohlenstoff-Atome = weiß, Sauerstoff-Atome = rot, Stickstoff-Atome = blau, Eisenatom = orange).<ref name="pmid18191143">PDB 2r5l; {{#invoke:Vorlage:Literatur|f}}{{#if: {{#if: Vorlage:Cite book/ParamBool Vorlage:Toter Link/archivebot Vorlage:Webarchiv/archiv-bot
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Andere Namen

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Vorhandene Strukturdaten: }}

Eigenschaften des menschlichen Proteins

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Masse/Länge Primärstruktur 612 aa

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Sekundär- bis Quartärstruktur

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Kofaktor Ca2+, Häm b

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Präkursor (712 aa)

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Isoformen

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Bezeichner
{{#if: | Gen-Namen | Gen-Name}} | Gen-Name(n) }}
Externe IDs 0 | }} - = – valid|1|2=/^[1-9]%d?%d?%d?%d?%d?%d?%d?%d?$/ 0 | Wikipedia:Vorlagenfehler/Vorlage:PubChem}} template= Vorlage:PubChem format=

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 }}

}}

Arzneistoffangaben
ATC-Code
 }}
 {{#if:|
DrugBank
Wirkstoffklasse
 }}

}}

Transporter-Klassifikation
TCDB
Bezeichnung
 }}

}}

{{#if:|Inhibitorklassifikation|{{#if:|Enzymklassifikationen|Enzymklassifikation}}}}
EC, Kategorie
MEROPS
MEROPS
Reaktionsart Redoxreaktion
 }}
Substrat Iodid, Bromid, Thiocyanat + H2O2
 }}
Produkte Hypoiodit, Hypobromit, Hypothiocyanit + H2O
 }}


}}

Vorkommen
{{#if: [ {{#if: Hovergen}}] [http://hogenom.univ-lyon1.fr/query_sequence?seq=P22079 {{#if: Hovergen}}]}} }} }}
Tiere }}
}}

}}

Mensch Hausmaus
Entrez
 {{ #if: 4025
4025 }}
 {{ #if: 76113
76113 }}
style="background:#C3FDB8; color:#202122;" | Ensembl
    {{ #if: ENSG00000167419
ENSG00000167419 }}
    {{ #if: ENSMUSG00000009356
ENSMUSG00000009356 }}

}

 |-
 | style="background:#C3FDB8; color:#202122;" | UniProt
 {{ #if: P22079
    | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|P22079}}{{#if:|Vorlage:Abrufdatum}}
    | |  }}
 {{ #if: Q5SW46
    | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q5SW46}}{{#if:|Vorlage:Abrufdatum}}
    | |  }}
 |-
 {{#if: NM_001160102NM_080420
    | | style="background:#C3FDB8; color:#202122;" | Refseq (mRNA)
      {{ #if: NM_001160102
         | | NM_001160102
         | |  }}
      {{ #if: NM_080420
         | | NM_080420
         | |  }}
    |}}
 |-
 {{#if: NP_001153574NP_536345
    | | style="background:#C3FDB8; color:#202122;" | Refseq (Protein)
      {{ #if: NP_001153574
         | | NP_001153574
         | |  }}
      {{ #if: NP_536345
         | | NP_536345
         | |  }}
    |}}
 |-
 {{#if: 175823773758268536118780642887826135
    | | style="background:#C3FDB8; color:#202122;" | Genlocus
      {{#if: 17 
        | {{#if: 58237737 
            | {{#if: 58268536 
                | |  #if:  |?db=|}}&position=chr17:58237737-58268536 Chr 17: {{#expr: 58237737 / 1000000 round 2}} – {{#expr: 58268536 / 1000000 round 2}} Mb 
                | |  }}
            | |  }}
        | |  }}
      {{#if: 11 
        | {{#if: 87806428 
            | {{#if: 87826135 
                | |  #if:  |?db=|}}&position=chr11:87806428-87826135 Chr 11: {{#expr: 87806428 / 1000000 round 2}} – {{#expr: 87826135 / 1000000 round 2}} Mb 
                | |  }}
           | |  }}
       | |  }}
    |}}
 |-
 | style="background:#C3FDB8; color:#202122;" | PubMed-Suche 
 {{ #if: 4025
    | | 4025
    | |  }}
 {{ #if: 76113
    | | 76113
    | |  }}

| |- | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe (Mensch) |- | style="background:#C3FDB8; color:#202122;" | Entrez | colspan="2" | 4025

 {{#if: ENSG00000167419
    | |-

| style="background:#C3FDB8; color:#202122;" | Ensembl | colspan="2" | ENSG00000167419 }} |- | style="background:#C3FDB8; color:#202122;" | UniProt | colspan="2" | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|P22079}}{{#if:|Vorlage:Abrufdatum}}

 {{#if: NM_001160102
    | |-

| style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) | colspan="2" | NM_001160102 }}

 {{#if: NP_001153574
    | |-

| style="background:#C3FDB8; color:#202122;" | Refseq (Protein) | colspan="2" | NP_001153574 }}

 {{#if: 17 
   | {{#if: 58237737 
       | {{#if: 58268536 
           | |-

| style="background:#C3FDB8; color:#202122;" | Genlocus | colspan="2" | #if: |?db=|}}&position=chr17:58237737-58268536 Chr 17: {{#expr: 58237737 / 1000000 round 2}} – {{#expr: 58268536 / 1000000 round 2}} Mb

           |  }}
       |  }}
   |  }}

|- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche | colspan="2" | 4025 }} {{#if: Hausmaus

    | {{#if: 76113ENSMUSG00000009356NM_080420NP_536345118780642887826135Q5SW46 
        |
        |  Spezies2= ist definiert, es sind jedoch keine weiteren Angaben zu Spezies2 vorhanden.{{#ifeq:0|0| }} }}
    | {{#if: 76113ENSMUSG00000009356NM_080420NP_536345118780642887826135Q5SW46 
        |  Es sind Angaben zu Spezies2 vorhanden, Spezies2= ist jedoch nicht definiert.{{#ifeq:0|0| }}
        |}}

}} | {{#if: Hausmaus | | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe

 |-
 | style="background:#C3FDB8; color:#202122;" |
 | style="background:#C3FDB8; color:#202122; text-align:center;" | Mensch
 | style="background:#C3FDB8; color:#202122; text-align:center;" | Hausmaus
 |-
 | style="background:#C3FDB8; color:#202122;" | Entrez
 {{ #if: 4025
    | | 4025
    | |  }}
 {{ #if: 76113
    | | 76113
    | |  }}
 |-
 {{#if: ENSG00000167419ENSMUSG00000009356
    | | style="background:#C3FDB8; color:#202122;" | Ensembl
    {{ #if: ENSG00000167419
       || ENSG00000167419
       ||  }}
    {{ #if: ENSMUSG00000009356
       || ENSMUSG00000009356
       ||  }}
  |}}
 |-
 | style="background:#C3FDB8; color:#202122;" | UniProt
 {{ #if: P22079
    | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|P22079}}{{#if:|Vorlage:Abrufdatum}}
    | |  }}
 {{ #if: Q5SW46
    | | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|Q5SW46}}{{#if:|Vorlage:Abrufdatum}}
    | |  }}
 |-
 {{#if: NM_001160102NM_080420
    | | style="background:#C3FDB8; color:#202122;" | Refseq (mRNA)
      {{ #if: NM_001160102
         | | NM_001160102
         | |  }}
      {{ #if: NM_080420
         | | NM_080420
         | |  }}
    |}}
 |-
 {{#if: NP_001153574NP_536345
    | | style="background:#C3FDB8; color:#202122;" | Refseq (Protein)
      {{ #if: NP_001153574
         | | NP_001153574
         | |  }}
      {{ #if: NP_536345
         | | NP_536345
         | |  }}
    |}}
 |-
 {{#if: 175823773758268536118780642887826135
    | | style="background:#C3FDB8; color:#202122;" | Genlocus
      {{#if: 17 
        | {{#if: 58237737 
            | {{#if: 58268536 
                | |  #if:  |?db=|}}&position=chr17:58237737-58268536 Chr 17: {{#expr: 58237737 / 1000000 round 2}} – {{#expr: 58268536 / 1000000 round 2}} Mb 
                | |  }}
            | |  }}
        | |  }}
      {{#if: 11 
        | {{#if: 87806428 
            | {{#if: 87826135 
                | |  #if:  |?db=|}}&position=chr11:87806428-87826135 Chr 11: {{#expr: 87806428 / 1000000 round 2}} – {{#expr: 87826135 / 1000000 round 2}} Mb 
                | |  }}
           | |  }}
       | |  }}
    |}}
 |-
 | style="background:#C3FDB8; color:#202122;" | PubMed-Suche 
 {{ #if: 4025
    | | 4025
    | |  }}
 {{ #if: 76113
    | | 76113
    | |  }}

| |- | colspan="3" style="background:#90EE90; color:#202122; text-align:center;" | Orthologe (Mensch) |- | style="background:#C3FDB8; color:#202122;" | Entrez | colspan="2" | 4025

 {{#if: ENSG00000167419
    | |-

| style="background:#C3FDB8; color:#202122;" | Ensembl | colspan="2" | ENSG00000167419 }} |- | style="background:#C3FDB8; color:#202122;" | UniProt | colspan="2" | {{#if: kurz| | UniProt }} {{#if:|{{{titel}}}|P22079}}{{#if:|Vorlage:Abrufdatum}}

 {{#if: NM_001160102
    | |-

| style="background:#C3FDB8; color:#202122;" | Refseq (mRNA) | colspan="2" | NM_001160102 }}

 {{#if: NP_001153574
    | |-

| style="background:#C3FDB8; color:#202122;" | Refseq (Protein) | colspan="2" | NP_001153574 }}

 {{#if: 17 
   | {{#if: 58237737 
       | {{#if: 58268536 
           | |-

| style="background:#C3FDB8; color:#202122;" | Genlocus | colspan="2" | #if: |?db=|}}&position=chr17:58237737-58268536 Chr 17: {{#expr: 58237737 / 1000000 round 2}} – {{#expr: 58268536 / 1000000 round 2}} Mb

           |  }}
       |  }}
   |  }}

|- | style="background:#C3FDB8; color:#202122;" | PubMed-Suche | colspan="2" | 4025 }} {{#if: Hausmaus

    | {{#if: 76113ENSMUSG00000009356NM_080420NP_536345118780642887826135Q5SW46 
        |
        |  Spezies2= ist definiert, es sind jedoch keine weiteren Angaben zu Spezies2 vorhanden.{{#ifeq:0|0| }} }}
    | {{#if: 76113ENSMUSG00000009356NM_080420NP_536345118780642887826135Q5SW46 
        |  Es sind Angaben zu Spezies2 vorhanden, Spezies2= ist jedoch nicht definiert.{{#ifeq:0|0| }}
        |}}

}} }}

|}{{#if:Lactoperoxidase 2R5L.png||}}

Das Enzym Lactoperoxidase (LPO) kommt in den meisten Tieren vor und wird im Menschen von den Brustdrüsen, Speicheldrüsen und Schleimdrüsen der Bronchien ausgeschieden. Es katalysiert die Oxidation von Phenolen und verschiedenen Anionen durch Wasserstoffperoxid. Die Reaktionsprodukte sind hochreaktive Moleküle, die toxisch auf in den Körper eingedrungene Mikroorganismen wirken. LPO ist daher ein Teil des angeborenen (unspezifischen) Immunsystems und ermöglicht die Neutralisierung von Bakterien in der Milch und anderen Schleimhautsekreten.<ref name="pmid6931123">{{#invoke:Vorlage:Literatur|f}}{{#if:

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Unter dem Lactoperoxidase-System versteht man die Kombination aus Lactoperoxidase und dessen ionischen Substraten, dem Wasserstoffperoxid sowie den Oxidationsprodukten. Bekannte Substrate sind Bromid- und Iodid-Ionen, aber auch das Thiocyanat-Ion. Die Produkte der enzymkatalysierten Oxidation sind stark antibakteriell wirksam, vermutlich durch Hemmung der Glucose-Aufnahme.<ref name="pmid9872115">{{#invoke:Vorlage:Literatur|f}}{{#if:

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Struktur

Die Struktur der Lactoperoxidase besteht hauptsächlich aus α-Helices. Hinzu kommen zwei kurze antiparallele β-Faltblätter. Ein Häm-Cofaktor befindet sich nahe dem Zentrum des Apoproteins.<ref name="pmid18191143" />

Funktion

Die Lactoperoxidase katalysiert die Oxidation verschiedener Sauerstoff-Akzeptoren durch Wasserstoffperoxid (H2O2):<ref name="de Wit_1996">{{#invoke:Vorlage:Literatur|f}}{{#if:

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  • reduzierter Akzeptor + H2O2 → oxidierter Akzeptor + H2O

Beispiele solcher Oxidationsreaktionen sind:

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Quelle des Wasserstoffperoxids ist vielfach die Reaktion von Glucose mit Sauerstoff in Gegenwart des Enzyms Glucose-Oxidase (EC 1.1.3.4), die ebenfalls im Speichel stattfindet. Die Glucose wiederum kann in Gegenwart des Speichel-Enzyms Amyloglucosidase (γ-Amylase (EC 3.2.1.3)) aus Stärke entstehen. Derartige Oxidationsprodukte sind hoch reaktiv und antibakteriell stark wirksam.<ref name="ISBN 0-8247-7298-9">{{#invoke:Vorlage:Literatur|f}}{{#if: | {{#if: Vorlage:Cite book/ParamBool | Vorlage:Toter Link/archivebot | Vorlage:Webarchiv/archiv-bot }}

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  }}</ref> Das Lactoperoxidase-System ist in der Lage, eine ganze Reihe von aerobischen<ref name="pmid18565914">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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Der Effekt des Lactoperoxidase-Systems hängt von bestimmten experimentellen Bedingungen ab. Wenn Bakterien unter aerobischen Bedingungen auf Nähragar kultiviert werden sollen, nachdem sie dem Lactoperoxidase-System ausgesetzt waren, wachsen sie nicht. Allerdings wachsen sie sehr wohl auf Blut-Agar unter anaerobischen Bedingungen.<ref name="pmid6724690" /> Das Lactoperoxidase-System scheint synergistisch mit Lactoferrin<ref name="pmid6345430">{{#invoke:Vorlage:Literatur|f}}{{#if:

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       | {{#if: Vorlage:Cite book/ParamBool
               | Vorlage:Toter Link/archivebot
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     | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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       | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
  }}Vorlage:Cite book/Meldung2{{#ifexpr: 0{{#ifeq:^^|^^||+1}}{{#ifeq:^^|^^||+1}}{{#ifeq:V. Roger, J. Tenovuo, M. Lenander-Lumikari, E. Söderling, P. Vilja|^^||+1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}</ref> zu agieren.

Ist Wasserstoffperoxid im Überschuss zum Thiocyanat vorhanden, kann das Lactoperoxidase-System auch cytotoxisch wirken.<ref name="pmid6724690">{{#invoke:Vorlage:Literatur|f}}{{#if:

       | {{#if: Vorlage:Cite book/ParamBool
               | Vorlage:Toter Link/archivebot
               | Vorlage:Webarchiv/archiv-bot
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     || Vorlage:Cite book/Meldung
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        | Vorlage:Cite book/Meldung
  }}{{#if: Vorlage:Cite book/ParamBool
     | Vorlage:Cite book/Meldung
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       | Vorlage:Cite book/Meldung
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    | Vorlage:Cite book/Meldung
  }}</ref>

Anwendungen

Aufgrund der antibakteriellen Wirksamkeit des Lactoperoxidase-Systems<ref name="Harper_2000">{{#invoke:Vorlage:Literatur|f}}{{#if: | {{#if: Vorlage:Cite book/ParamBool | Vorlage:Toter Link/archivebot | Vorlage:Webarchiv/archiv-bot }}

  }}{{#invoke:TemplatePar|check

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  }}Vorlage:Cite book/URLVorlage:Cite book/Meldung2{{#if: Vorlage:Cite book/ParamBool
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| Vorlage:Cite book/Meldung

  }}{{#if: Vorlage:Cite book/ParamBool
     | Vorlage:Cite book/Meldung
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| Vorlage:Cite book/Meldung

  }}{{#if: Vorlage:Cite book/ParamBool

| Vorlage:Cite book/Meldung

  }}{{#if: Vorlage:Cite book/ParamBool

| Vorlage:Cite book/Meldung

  }}{{#if:  Vorlage:Cite book/ParamBool
     | Vorlage:Cite book/Meldung
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  }}{{#ifexpr: {{#ifeq:^^|^^|0|1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}{{#ifexpr: {{#ifeq:^^|^^|0|1}}{{#ifeq:54|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}{{#ifexpr: {{#ifeq:^^|^^|0|1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}{{#ifexpr: {{#ifeq:^^|^^|0|1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}{{#ifexpr: {{#ifeq:^^|^^|0|1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}</ref> wird es zur Konservierung von Nahrungsmitteln und Kosmetika sowie in der Augenheilkunde eingesetzt. Weitere Anwendungen finden sich in den Bereichen Zahnheilkunde und Wundbehandlung. Möglicherweise kann das Lactoperoxidase-System auch zur Bekämpfung von Tumoren und Viren eingesetzt werden.<ref name="pmid2790777">{{#invoke:Vorlage:Literatur|f}}{{#if: 
       | {{#if: Vorlage:Cite book/ParamBool
               | Vorlage:Toter Link/archivebot
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    | Vorlage:Cite book/Meldung
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    | Vorlage:Cite book/Meldung
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        | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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    | Vorlage:Cite book/Meldung
  }}</ref>

Milch und Milchprodukte

Das Lactoperoxidase-System hemmt das Wachstum der bakteriellen Flora in der Milch und in Milchprodukten.<ref name="Reiter_1984">{{#invoke:Vorlage:Literatur|f}}{{#if:

       | {{#if: Vorlage:Cite book/ParamBool
               | Vorlage:Toter Link/archivebot
               | Vorlage:Webarchiv/archiv-bot
         }}
  }}{{#invoke:TemplatePar|check
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  }}Vorlage:Cite book/URL{{#if:  | Vorlage:Cite book/Meldung }}{{#if:        | Vorlage:Cite book/Meldung }}{{#if: Dairy Ind. Int.
     || Vorlage:Cite book/Meldung
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        | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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       | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
  }}Vorlage:Cite book/Meldung2{{#ifexpr: 0{{#ifeq:^^|^^||+1}}{{#ifeq:^^|^^||+1}}{{#ifeq:B. Reiter, BG Härnulv|^^||+1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}</ref> Die Zugabe von Wasserstoffperoxid und einem Thiocyanat verlängert die Haltbarkeit gekühlter Rohmilch.<ref name="de Wit_1996" /><ref name="Zajac_1983a">{{#invoke:Vorlage:Literatur|f}}{{#if: 
       | {{#if: Vorlage:Cite book/ParamBool
               | Vorlage:Toter Link/archivebot
               | Vorlage:Webarchiv/archiv-bot
         }}
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Zahnheilkunde

Das Lactoperoxidase-System scheint auch zur Behandlung von Karies, Gingivitis und Parodontitis geeignet zu sein<ref name="Poulson OM">{{#if:{{#ifexpr:{{#if:WO|0|1}} or {{#if:1988002600|0|1}}|1}}|Fehlender Parameter {{#if:WO||„Land“{{#if:1988002600|| und }}}}{{#if:1988002600||„V-Nr“}}|}}{{#if: {{#invoke:Expr|TemplateBooland}}|{{#ifeq:Patentanmeldung|Patentanmeldung|Patentanmeldung|{{#ifeq:Patentanmeldung|Gebrauchsmuster|Gebrauchsmuster|Patent}}}} {{#if:{{#invoke:TemplUtl|faculty|}}|WO1988002600|{{#switch: {{{DB}}} | DEPATIS =WO1988002600 | WIPO = WO1988002600 | Google = WO1988002600 | #default =WO1988002600 }}}}{{#if:Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition1988-04-21Poulson OM|:|.}}{{#if:Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition| Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition.}}{{#if:1988-04-21| Angemeldet am {{#iferror:{{#invoke:Vorlage:FormatDate|Execute}}|}}{{#if:Poulson OM|,}}}}{{#if:|{{#if:1988-04-21| veröffentlicht am | Veröffentlicht am }}{{#iferror:{{#invoke:Vorlage:FormatDate|Execute}}|}}{{#if:Poulson OM|,}}}}{{#if:| Anmelder: {{#if:Poulson OM|,}}}}{{#if:Poulson OM| Erfinder: Poulson OM}}{{#if:| ()}}{{#if:1988-04-21Poulson OM|.}}}}{{#invoke:TemplatePar|match |template= Vorlage:Patent |cat= {{#ifeq: 0 | 0 | Wikipedia:Vorlagenfehler/Vorlage:Patent}} |format= |preview=@@@ |1=Land= ABC+ |2=V-Nr= /^[0-9A-Z]+$/ |3=Titel= * |4=Erfinder= * |5=Anmelder= * |6=A-Datum= * |7=V-Datum= * |8=Typ= ASCII |9=Code= ASCII |10=Kommentar= * |11=KeinLink= ASCII |12=DB=ASCII }}</ref> und wird daher als Bestandteil von Zahnpasten und Mundspüllösungen eingesetzt. Weil es das Bakterienwachstum in der Mundhöhle hemmt, hemmt es auch die Säureproduktion dieser Bakterien.<ref name="Hoogedoorn_1985">{{#invoke:Vorlage:Literatur|f}}{{#if: | {{#if: Vorlage:Cite book/ParamBool | Vorlage:Toter Link/archivebot | Vorlage:Webarchiv/archiv-bot }}

  }}{{#invoke:TemplatePar|check

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Klinische Bedeutung des Lactoperoxidase-Systems

Zahn- und Mundgesundheit

In den letzten Jahrzehnten sind eine Reihe von klinischen Studien zur Wirksamkeit des Lactoperoxidase-Systems in verschiedenen Mundhygiene-Produkten (Zahnpasten, Mundspüllösungen) veröffentlicht worden. Nachdem indirekt über die Messung experimenteller Gingivitis- und Karies-Parameter gezeigt worden war, dass Mundspüllösungen,<ref name="pmid4522423">{{#invoke:Vorlage:Literatur|f}}{{#if:

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  }}</ref> welche Amyloglucosidase (γ-Amylase) und Glucose-Oxidase enthalten, das Lactoperoxidase-System aktivieren, sind aus jüngster Zeit Studien bekannt, die den Mechanismus der Schutzfunktion von Enzymen in Mundhygieneprodukten beleuchten. So werden Enzyme wie Lysozym, Lactoperoxidase und Glucose-Oxidase von den Zahnpasten auf das Pellikel übertragen. Als Bestandteil des Pellikels sind diese Enzyme katalytisch hoch aktiv.<ref name="pmid20417500">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> Ebenso hat das Lactoperoxidase-System als Bestandteil von Zahnpasten einen günstigen Einfluss auf die Vermeidung frühkindlicher Karies,<ref name="pmid19725235">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> indem es die Zahl gebildeter Kolonien kariogener Mikroflora herabsetzt, während gleichzeitig die Thiocyanat-Konzentration steigt. Zahnpasten mit dem Lactoperoxidase-System erwiesen sich bei Xerostomie-Patienten im Vergleich zu fluoridhaltigen Zahnpasten hinsichtlich Plaque-Bildung und Zahnfleischentzündungen als überlegen.<ref name="pmid8063434-1">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> nicht zuletzt um den Mechanismus der Schutzwirkung näher zu beleuchten, welcher noch nicht genau aufgeklärt ist.<ref name="pmid7887144">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> Die Anwendung von Lactoperoxidase ist nicht auf Karies, Gingivitis und Parodontitis beschränkt.<ref name="pmid20701667">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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    | Vorlage:Cite book/Meldung
  }}</ref> So kann eine Kombination aus Lysozym und Lactoperoxidase auch zur unterstützenden Behandlung des Burning Mouth Syndroms (Glossodynie) eingesetzt werden. In Kombination mit Lactoferrin wirkt Lactoperoxidase gegen Mundgeruch,<ref name="pmid20512389">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> in Kombination mit Lactoferrin und Lysozym trägt Lactoperoxidase zur Linderung von Beschwerden wegen Mundtrockenheit (Xerostomie) bei.<ref name="pmid18194332">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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  }}</ref> Ebenso können Gele mit Lactoperoxidase bei Mundhöhlenkrebs-Patienten, deren Speichelfluss infolge von Bestrahlungen eingeschränkt ist (Xerostomie), zur Symptomlinderung beitragen und gleichzeitig die Bakterienflora günstig beeinflussen.<ref name="pmid17912104">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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    | Vorlage:Cite book/Meldung
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Zystische Fibrose

Im Speichel von Patienten mit zystischer Fibrose wird weniger Thiocyanat gefunden als in gesunden Patienten.<ref name="pmid19918082">{{#invoke:Vorlage:Literatur|f}}{{#if:

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     || Vorlage:Cite book/Meldung
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       | Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
  }}Vorlage:Cite book/Meldung2{{#ifexpr: 0{{#ifeq:^^|^^||+1}}{{#ifeq:^^|^^||+1}}{{#ifeq:Y. Xu, S. Szép, Z. Lu|^^||+1}}{{#ifeq:^^|^^||+1}} > 1
    | Vorlage:Cite book/Meldung
  }}</ref> Weil so auch weniger antibakteriell wirksames Hypothiocyanit gebildet werden kann, könnte dies ein Grund dafür sein, dass diese Patienten gehäuft unter Atemwegserkrankungen leiden.<ref name="pmid17082494">{{#invoke:Vorlage:Literatur|f}}{{#if: 
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     || Vorlage:Cite book/Meldung
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     | Vorlage:Cite book/Meldung
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    | Vorlage:Cite book/Meldung
  }}</ref>

Krebs

Antikörper-Konjugate mit Lactoperoxidase töten Tumorzellen ab.<ref name="pmid2790777" /> Makrophagen, die Lactoperoxidase ausgesetzt waren, können Tumorzellen verstärkt neutralisieren.<ref name="pmid2402192" /> Die Oxidation von Estradiol durch Lactoperoxidase wird als mögliche Quelle für oxidativen Stress bei Brustkrebs gehandelt.<ref name="pmid7955118">{{#invoke:Vorlage:Literatur|f}}{{#if:

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Weblinks

Einzelnachweise

<references />