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- Title
Homology between the Primary Structures of β-Lactoglobulins and Human Retinol-Binding Protein: Evidence for a Similar Biological Function?
- Authors
GODOVAC-ZIMMERMANN, Jasminka; CONTI, Amedeo; LIBERATORI, Jone; BRAUNITZER, Gerhard
- Abstract
Two types of β-lactoglobulins were identified and isolated from horse colostrum: β-lg I and β-lg II. The amino-acid sequence of some tryptic peptides from the new monomeric β-lactoglobulin II was determined and aligned to the other β-lactoglobulins of known sequence and to the human plasma retinol-binding protein. The comparison of the primary structures of β-lactoglobulins and human retinol-binding protein shows an unexpectedly high homology of 25%. We found 37 identities among 149 possible homologous residues. Among them is a tryptophan residue at position 19 of β-lg which might represent the binding site of β-ionone. These data suggest a common origin of β-lactoglobulin and human retinol-binding protein and imply that β-lactoglobulins may be involved in the metabolism of retinol.
- Publication
Biological Chemistry, 1985, Vol 366, Issue 1, p431
- ISSN
1431-6730
- Publication type
Article