Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1977-7-23
pubmed:abstractText
A folate-binding protein has been solubilized from Lactobacillus casei by treatment of membrane preparations with Triton X-100 in the presence of [3H]folate. The protein-folate complex was purified 100-fold and recovered in a 22% yield by adsorption and elution from microgranular silica (Quso G-32), followed by passage through Sephadex G-150. When subjected to sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the purified preparations showed only a single, protein-staining band whose molecular weight was 25,000. Bound folate (34 nmol/mg of protein) corresponded to 0.85 mol/mol of protein. Analyses of the protein revealed relatively few charged or polar amino acids, an unusually high content of hydrophobic residues and methionine, and the absence of cysteine. The purified protein-folate complex was contained within a Triton micelle (molecular weight, 220,000; about 340 mol of detergent per mol of protein). Bound folate was retained when the micelle was exposed at 4 degrees to solutions whose pH values ranged between 3 and 12; at 23 degrees, however, stability was decreased, especially above pH 8. Folate could be released by treatment of the micelle with ethanol or with chaotropic agents such as guanidinium chloride, perchlorate, or thiocyanate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3760-5
pubmed:dateRevised
2009-10-27
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Purification and properties of a membrane-associated, folate-binding protein from Lactobacillus casei.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.