Purification and properties of a membrane-associated, folate-binding protein from Lactobacillus casei.

@article{Henderson1977PurificationAP,
  title={Purification and properties of a membrane-associated, folate-binding protein from Lactobacillus casei.},
  author={Gary B. Henderson and Edward M. Zevely and Frank M. Huennekens},
  journal={The Journal of biological chemistry},
  year={1977},
  volume={252 11},
  pages={
          3760-5
        }
}

Partial purification and characterization of a folatebinding protein from human choroid plexus

A folate-binding protein (binder) from human choroid plexus was solubilized with Triton X-100 and partially purified in three steps: affinity chromatography, Sephadex G-200 column Chromatography, and polyacrylamide gel electrophoresis, and the binding activity was located in the region of the gel with a molecular weight between 45,000 and 60,000.

Cation-Dependent Binding of Substrate to the Folate Transport Protein of Lactobacillus casei

The results suggest that the folate transport protein of L. casei may contain both a substrate- and cation-binding site and that folate binds with a high affinity only after the cation -binding site has been occupied.

Isolation and characterization of the folate-binding protein from cow's milk

The folate-binding protein from cow's milk has been purified in milligramme scale by combination of ion-exchange chromatography and affinity chromatography, and the amino acid composition is compatible with this value.

Methotrexate-Resistant Subline of Lactobacillus caseit

Findings indicate that the mutant binding protein exists in a low-affinity form due to disulfide bridge formation between two homologous protein subunits and that cleavage of this bond by mercaptoethanol generates the high-Affinity state.

Multiple folate transport systems in L1210 cells.

Diglyceride Kinase from Escherichia coli

The diglyceride kinase activity of membranes from Escherichia coli was extracted into acidic butan-1-ol and the purified enzyme was devoid of lipid, and it required re-addition of lipid for activity.

Kinetic evidence for two interconvertible forms of the folate transport protein from Lactobacillus casei

F folate transport protein of L. casei exists in two forms which can be distinguished by the accessibility of the binding site to the external medium and whose amounts are dependent upon the presence of bound folate, the pH, and the energetic state of the cell.
...