Document Detail


Conversion of an apparent 100 kDa folate binding protein from human milk to a 25 kDa molecular species by phospholipase D.
MedLine Citation:
PMID:  1794957     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Gel filtration studies in the presence of Triton X-100 showed that treatment with phospholipase D reduced the apparent molecular size of the 100 kDa folate binding protein from human milk to 25 kDa, which is the molecular size of the low molecular weight folate binding protein. A phospholipase D induced cleavage of a hydrophobic phospholipid domain inserting the protein into Triton X-100 micelles could account for this phenomenon.
Authors:
S I Hansen; J Holm
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition     Volume:  61     ISSN:  0300-9831     ISO Abbreviation:  Int J Vitam Nutr Res     Publication Date:  1991  
Date Detail:
Created Date:  1992-04-08     Completed Date:  1992-04-08     Revised Date:  2007-02-21    
Medline Journal Info:
Nlm Unique ID:  1273304     Medline TA:  Int J Vitam Nutr Res     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  264-7     Citation Subset:  IM    
Affiliation:
Department of Clinical Chemistry, Central Hospital Hillerød, Denmark.
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MeSH Terms
Descriptor/Qualifier:
Carrier Proteins / metabolism*
Folic Acid / metabolism*
Humans
Milk Proteins / metabolism*
Molecular Weight
Phospholipase D / metabolism*
Receptors, Cell Surface*
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Milk Proteins; 0/Receptors, Cell Surface; 0/folate-binding protein; 59-30-3/Folic Acid; EC 3.1.4.4/Phospholipase D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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