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Structural requirements for anion substrates of the methotrexate transport system in L1210 cells.
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Affinity labeling of the 5-methyltetrahydrofolate/methotrexate transport protein of L1210 cells by treatment with an N-hydroxysuccinimide ester of [3H]methotrexate.
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Transport routes utilized by L1210 cells for the influx and efflux of methotrexate.
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Anion exchange mechanism for transport of methotrexate in L1210 cells.
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Transport of methotrexate in L1210 cells: effect of ions on the rate and extent of uptake.
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Mechanism of Folate Transport in Lactobacillus casei: Evidence for a Component Shared with the Thiamine and Biotin Transport Systems
TLDR
The results are consistent with the hypothesis that the folate, thiamine, and biotin transport systems of L. casei each function via a specific binding protein, and that they require, in addition, a common component present in limiting amounts per cell.
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Use of non-physiological buffer systems in the analysis of methotrexate transport in L1210 cells.
TLDR
The results suggest that the integrity of L1210 cells is not adversely affected by either the presence of HEPES in the suspending medium or by the absence of certain physiological ions, and that methotrexate transport parameters measured under these conditions can nevertheless provide meaningful information on the properties and mechanism of this transport system.
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Purification and properties of a membrane-associated, folate-binding protein from Lactobacillus casei.
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Binding properties of the 5-methyltetrahydrofolate/methotrexate transport system in L1210 cells.
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The folate and thiamine transport proteins of Lactobacillus casei.
TLDR
Two separate binding proteins, one specific for folate and the other for thiamine, have been isolated from membrane fragments of Lactobacillus casei and the ability of these compounds to inhibit the transport of the corresponding vitamins is paralleled by their ability to inhibit binding.
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