scholarly journals Improved folding of apo-retinol-binding protein in the periplasm of Escherichia coli: positive influences of dsbC coexpression and of an amino acid exchange in the vitamin A binding site

1998 ◽  
Vol 11 (7) ◽  
pp. 601-607 ◽  
Author(s):  
A. M. Schmidt ◽  
I. Bloss ◽  
A. Skerra
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Vitamin A ◽  
Binding Site ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Amino Acid Exchange ◽  
Acid Exchange

Low plasma concentrations of retinol-binding protein in individuals with mutations affecting position 84 of the transthyretin molecule

1995 ◽  
Vol 41 (9) ◽  
pp. 1288-1291 ◽  
Author(s):  
R P Waits ◽  
T Yamada ◽  
T Uemichi ◽  
M D Benson
Keyword(s):  
Amino Acid ◽  
Vitamin A ◽  
Binding Protein ◽  
Plasma Concentrations ◽  
Substantial Reduction ◽  
Point Mutations ◽  
Gene Mutations ◽  
Retinol Binding Protein ◽  
Single Amino Acid ◽  
Amino Acid Substitutions

Abstract Retinol-binding protein (RBP), the principal carrier for vitamin A, is known to form a complex with transthyretin (TTR) for transport in plasma. Individuals from a kindred with the amino acid substitution of serine for isoleucine at position 84 (Ser84) of the TTR molecule show substantial reduction in plasma concentrations of RBP. In the present study, we measured plasma RBP in individuals from several kindreds, demonstrating 17 different point mutations within the TTR gene. In each case, these mutations caused single amino acid substitutions at various positions throughout the TTR molecule. Of all the individuals examined, only those with mutations causing amino acid substitutions at position 84 of the TTR molecule (Ser84 and Asn84) demonstrated substantial decreases in plasma concentrations of RBP. These results suggest that the isoleucine at position 84 on the TTR molecule may be critically involved in mediating RBP binding. Further, these findings demonstrate the importance of considering TTR gene mutations when clinically evaluating patients with low RBP.

scholarly journals The Effects of Chylomicron Vitamin A on the Metabolism of Retinol-binding Protein in the Rat

1973 ◽  
Vol 248 (5) ◽  
pp. 1544-1549 ◽  
Author(s):  
John Edgar Smith ◽  
Yasutoshi Muto ◽  
Peter O. Milch ◽  
DeWitt S. Goodman
Keyword(s):  
Vitamin A ◽  
Binding Protein ◽  
Retinol Binding Protein
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