Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin

Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been...

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Veröffentlicht in:Experimental parasitology 1996-07, Vol.83 (2), p.216-228
Hauptverfasser: Tachezy, Jan, Kulda, Jaroslav, Bahnı́ková, Ivana, Suchan, Pavel, Rázga, Jakub, Schrével, Joseph
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container_issue 2
container_start_page 216
container_title Experimental parasitology
container_volume 83
creator Tachezy, Jan
Kulda, Jaroslav
Bahnı́ková, Ivana
Suchan, Pavel
Rázga, Jakub
Schrével, Joseph
description Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.
doi_str_mv 10.1006/expr.1996.0068
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Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. 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Molecular biology ; BIODISPONIBILIDAD ; BIODISPONIBILITE ; Biological and medical sciences ; Cattle ; CRECIMIENTO ; CROISSANCE ; EDTA, ethylendiaminetetracetic acid ; endocytosis ; ENZYMIC ACTIVITY ; EXPERIMENTACION IN VITRO ; EXPERIMENTATION IN VITRO ; FER ; Ferric Compounds - pharmacology ; Fundamental and applied biological sciences. Psychology ; GROWTH ; HIERRO ; Hydrogen-Ion Concentration ; HYDROGENASE ; hydrogenase (EC 1.18.3.1) ; Hydrogenase - metabolism ; IN VITRO EXPERIMENTATION ; IRON ; Iron - metabolism ; Iron Chelating Agents - pharmacology ; Ketone Oxidoreductases - metabolism ; LACTOFERRIN ; Lactoferrin - metabolism ; lactoferrin and transferrin-dependent iron uptake ; lactoferrin-specific receptors ; LACTOFERRINAS ; LACTOFERRINE ; Ligands ; Male ; Mice ; MODE OF ACTION ; Nitrilotriacetic Acid - analogs &amp; derivatives ; Nitrilotriacetic Acid - pharmacology ; OXIDOREDUCTASES ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; PBS, phosphate-buffered saline ; PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1) ; Protozoa ; Pyruvate Synthase ; Receptors, Cell Surface - metabolism ; Receptors, Transferrin - metabolism ; SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis ; Temperature ; Transferrin - metabolism ; TRANSFERRINAS ; TRANSFERRINE ; TRANSFERRINS ; TRITRICHOMONAS FOETUS ; Tritrichomonas foetus - drug effects ; Tritrichomonas foetus - growth &amp; development ; Tritrichomonas foetus - metabolism ; TYM, trypticase–yeast extract–maltose ; UPTAKE</subject><ispartof>Experimental parasitology, 1996-07, Vol.83 (2), p.216-228</ispartof><rights>1996 Academic Press</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-1c41a639500dc6af679d3b99a1c2f02cb1ae2c04da871dbc0862c21074d56e373</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014489496900685$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=3195989$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8682190$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tachezy, Jan</creatorcontrib><creatorcontrib>Kulda, Jaroslav</creatorcontrib><creatorcontrib>Bahnı́ková, Ivana</creatorcontrib><creatorcontrib>Suchan, Pavel</creatorcontrib><creatorcontrib>Rázga, Jakub</creatorcontrib><creatorcontrib>Schrével, Joseph</creatorcontrib><title>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</title><title>Experimental parasitology</title><addtitle>Exp Parasitol</addtitle><description>Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.</description><subject>2,2'-Dipyridyl - pharmacology</subject><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Animals</subject><subject>BIOAVAILABILITY</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>BIODISPONIBILIDAD</subject><subject>BIODISPONIBILITE</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>CRECIMIENTO</subject><subject>CROISSANCE</subject><subject>EDTA, ethylendiaminetetracetic acid</subject><subject>endocytosis</subject><subject>ENZYMIC ACTIVITY</subject><subject>EXPERIMENTACION IN VITRO</subject><subject>EXPERIMENTATION IN VITRO</subject><subject>FER</subject><subject>Ferric Compounds - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GROWTH</subject><subject>HIERRO</subject><subject>Hydrogen-Ion Concentration</subject><subject>HYDROGENASE</subject><subject>hydrogenase (EC 1.18.3.1)</subject><subject>Hydrogenase - metabolism</subject><subject>IN VITRO EXPERIMENTATION</subject><subject>IRON</subject><subject>Iron - metabolism</subject><subject>Iron Chelating Agents - pharmacology</subject><subject>Ketone Oxidoreductases - metabolism</subject><subject>LACTOFERRIN</subject><subject>Lactoferrin - metabolism</subject><subject>lactoferrin and transferrin-dependent iron uptake</subject><subject>lactoferrin-specific receptors</subject><subject>LACTOFERRINAS</subject><subject>LACTOFERRINE</subject><subject>Ligands</subject><subject>Male</subject><subject>Mice</subject><subject>MODE OF ACTION</subject><subject>Nitrilotriacetic Acid - analogs &amp; derivatives</subject><subject>Nitrilotriacetic Acid - pharmacology</subject><subject>OXIDOREDUCTASES</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>PBS, phosphate-buffered saline</subject><subject>PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1)</subject><subject>Protozoa</subject><subject>Pyruvate Synthase</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Transferrin - metabolism</subject><subject>SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis</subject><subject>Temperature</subject><subject>Transferrin - metabolism</subject><subject>TRANSFERRINAS</subject><subject>TRANSFERRINE</subject><subject>TRANSFERRINS</subject><subject>TRITRICHOMONAS FOETUS</subject><subject>Tritrichomonas foetus - drug effects</subject><subject>Tritrichomonas foetus - growth &amp; development</subject><subject>Tritrichomonas foetus - metabolism</subject><subject>TYM, trypticase–yeast extract–maltose</subject><subject>UPTAKE</subject><issn>0014-4894</issn><issn>1090-2449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAQhq0KVLYfVw5ISDmg3rLMOF7H5lZVUCqtxIHt2fKOnWK0ibd2UsG_x1FWvXHyjN7HY8_D2HuENQLIz_7PMa1Ra7kunTpjKwQNNRdCv2ErABS1UFq8Yxc5_wYAhVycs3MlFUcNK3a_S2FMgX7FPg42V13045S_PKQ4VLf0PIUcxlDqLsW-2loaY-dTCkNlB1ftkh3y0l-xt509ZH99Oi_Z47evu7vv9fbH_cPd7bYmIdqxRhJoZaM3AI6k7WSrXbPX2iLxDjjt0XpOIJxVLbo9gZKcOEIr3Eb6pm0u2c0y95ji8-TzaPqQyR8OdvBxygalaOUGeQHXC0gp5px8Z44p9Db9NQhmNmdmc2Y2Z2Zz5cLH0-Rp33v3ip9UlfzTKbeZ7KEru1PIr1iDeqOVLtiHBetsNPYpFeTxp24BUcxvqCX0RdFL8MlkCn4g70LyNBoXw_--9w_uCZKT</recordid><startdate>19960701</startdate><enddate>19960701</enddate><creator>Tachezy, Jan</creator><creator>Kulda, Jaroslav</creator><creator>Bahnı́ková, Ivana</creator><creator>Suchan, Pavel</creator><creator>Rázga, Jakub</creator><creator>Schrével, Joseph</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope></search><sort><creationdate>19960701</creationdate><title>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</title><author>Tachezy, Jan ; Kulda, Jaroslav ; Bahnı́ková, Ivana ; Suchan, Pavel ; Rázga, Jakub ; Schrével, Joseph</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-1c41a639500dc6af679d3b99a1c2f02cb1ae2c04da871dbc0862c21074d56e373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>2,2'-Dipyridyl - pharmacology</topic><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Animals</topic><topic>BIOAVAILABILITY</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>BIODISPONIBILIDAD</topic><topic>BIODISPONIBILITE</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>CRECIMIENTO</topic><topic>CROISSANCE</topic><topic>EDTA, ethylendiaminetetracetic acid</topic><topic>endocytosis</topic><topic>ENZYMIC ACTIVITY</topic><topic>EXPERIMENTACION IN VITRO</topic><topic>EXPERIMENTATION IN VITRO</topic><topic>FER</topic><topic>Ferric Compounds - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GROWTH</topic><topic>HIERRO</topic><topic>Hydrogen-Ion Concentration</topic><topic>HYDROGENASE</topic><topic>hydrogenase (EC 1.18.3.1)</topic><topic>Hydrogenase - metabolism</topic><topic>IN VITRO EXPERIMENTATION</topic><topic>IRON</topic><topic>Iron - metabolism</topic><topic>Iron Chelating Agents - pharmacology</topic><topic>Ketone Oxidoreductases - metabolism</topic><topic>LACTOFERRIN</topic><topic>Lactoferrin - metabolism</topic><topic>lactoferrin and transferrin-dependent iron uptake</topic><topic>lactoferrin-specific receptors</topic><topic>LACTOFERRINAS</topic><topic>LACTOFERRINE</topic><topic>Ligands</topic><topic>Male</topic><topic>Mice</topic><topic>MODE OF ACTION</topic><topic>Nitrilotriacetic Acid - analogs &amp; derivatives</topic><topic>Nitrilotriacetic Acid - pharmacology</topic><topic>OXIDOREDUCTASES</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>PBS, phosphate-buffered saline</topic><topic>PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1)</topic><topic>Protozoa</topic><topic>Pyruvate Synthase</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Transferrin - metabolism</topic><topic>SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis</topic><topic>Temperature</topic><topic>Transferrin - metabolism</topic><topic>TRANSFERRINAS</topic><topic>TRANSFERRINE</topic><topic>TRANSFERRINS</topic><topic>TRITRICHOMONAS FOETUS</topic><topic>Tritrichomonas foetus - drug effects</topic><topic>Tritrichomonas foetus - growth &amp; development</topic><topic>Tritrichomonas foetus - metabolism</topic><topic>TYM, trypticase–yeast extract–maltose</topic><topic>UPTAKE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tachezy, Jan</creatorcontrib><creatorcontrib>Kulda, Jaroslav</creatorcontrib><creatorcontrib>Bahnı́ková, Ivana</creatorcontrib><creatorcontrib>Suchan, Pavel</creatorcontrib><creatorcontrib>Rázga, Jakub</creatorcontrib><creatorcontrib>Schrével, Joseph</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Experimental parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tachezy, Jan</au><au>Kulda, Jaroslav</au><au>Bahnı́ková, Ivana</au><au>Suchan, Pavel</au><au>Rázga, Jakub</au><au>Schrével, Joseph</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin</atitle><jtitle>Experimental parasitology</jtitle><addtitle>Exp Parasitol</addtitle><date>1996-07-01</date><risdate>1996</risdate><volume>83</volume><issue>2</issue><spage>216</spage><epage>228</epage><pages>216-228</pages><issn>0014-4894</issn><eissn>1090-2449</eissn><coden>EXPAAA</coden><abstract>Tachezy, J., Kulda, J., Bahnı́ková, I., Suchan, P., Rázga, J., and Schrével, J. 1996.Tritrichomonas foetus:Iron acquisition from lactoferrin and transferrin.Experimental Parasitology83,216–228. Acquisition of iron from lactoferrin and transferrin by a parasitic protozoonTritrichomonas foetushas been studiedin vitro.Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane ofT. foetusat 4°C was demonstrated for125I-labeled lactoferrin only. About 1.7 × 105binding sites of a single class withKd≅ 3.6 μMwas estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37°C. The cell-associated radioactivity after 30 min incubation of the parasite with125I-lactoferrin at 37°C was about 3.5-fold higher than the amount bound at 4°C. The majority of internalized125I-lactoferrin was released within 15 min of cell reincubation at 37°C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of125I-transferrin was nonspecific and did not display saturable kinetics. The growth ofT. foetusin iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37°C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate thatT. foetusis able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>8682190</pmid><doi>10.1006/expr.1996.0068</doi><tpages>13</tpages></addata></record>
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identifier ISSN: 0014-4894
ispartof Experimental parasitology, 1996-07, Vol.83 (2), p.216-228
issn 0014-4894
1090-2449
language eng
recordid cdi_proquest_miscellaneous_16476512
source MEDLINE; Elsevier ScienceDirect Journals
subjects 2,2'-Dipyridyl - pharmacology
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Animals
BIOAVAILABILITY
Biochemistry. Physiology. Immunology. Molecular biology
BIODISPONIBILIDAD
BIODISPONIBILITE
Biological and medical sciences
Cattle
CRECIMIENTO
CROISSANCE
EDTA, ethylendiaminetetracetic acid
endocytosis
ENZYMIC ACTIVITY
EXPERIMENTACION IN VITRO
EXPERIMENTATION IN VITRO
FER
Ferric Compounds - pharmacology
Fundamental and applied biological sciences. Psychology
GROWTH
HIERRO
Hydrogen-Ion Concentration
HYDROGENASE
hydrogenase (EC 1.18.3.1)
Hydrogenase - metabolism
IN VITRO EXPERIMENTATION
IRON
Iron - metabolism
Iron Chelating Agents - pharmacology
Ketone Oxidoreductases - metabolism
LACTOFERRIN
Lactoferrin - metabolism
lactoferrin and transferrin-dependent iron uptake
lactoferrin-specific receptors
LACTOFERRINAS
LACTOFERRINE
Ligands
Male
Mice
MODE OF ACTION
Nitrilotriacetic Acid - analogs & derivatives
Nitrilotriacetic Acid - pharmacology
OXIDOREDUCTASES
OXIDORREDUCTASAS
OXYDOREDUCTASE
PBS, phosphate-buffered saline
PFOR, pyruvate:ferredoxin oxidoreductase (EC 1.2.7.1)
Protozoa
Pyruvate Synthase
Receptors, Cell Surface - metabolism
Receptors, Transferrin - metabolism
SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis
Temperature
Transferrin - metabolism
TRANSFERRINAS
TRANSFERRINE
TRANSFERRINS
TRITRICHOMONAS FOETUS
Tritrichomonas foetus - drug effects
Tritrichomonas foetus - growth & development
Tritrichomonas foetus - metabolism
TYM, trypticase–yeast extract–maltose
UPTAKE
title Tritrichomonas foetus:Iron Acquisition from Lactoferrin and Transferrin
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