PMID- 3997791
OWN - NLM
STAT- MEDLINE
DCOM- 19850708
LR  - 20190511
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 97
IP  - 1
DP  - 1985 Jan
TI  - Comparison of the amino acid sequences of hen plasma-, yolk-, and 
      white-riboflavin binding proteins.
PG  - 19-28
AB  - The amino acid sequence of hen egg yolk-riboflavin binding protein (yolk-RBP) was 
      determined by conventional methods. The sequence was identical with that of hen 
      egg white-riboflavin binding protein except that their carboxyltermini were 
      different, that of yolk-RBP lacked 11 or 13 amino acid residues, while hen 
      plasma-RBP had the same C-terminal sequence as white-RBP. This indicated that the 
      C-terminal 11 or 13 amino acid residues in plasma-RBP might be cleaved off during 
      the incorporation from the blood into the oocyte or in the yolk fluid. Yolk-RBP 
      had the same characteristics as white-RBP, such as N-terminal pyroglutamic acid, 
      polymorphism in the amino acid sequence (Lys/Asn) at the fourteenth residue from 
      the N-terminal end, carbohydrate chains attached to both Asn(36) and Asn(147) 
      residues, and phosphate groups bound to some serine residues in the sequence of 
      Ser(185) to Ser(197) as a cluster. These results led us to the conclusion that 
      yolk- and white-RBPs are bio-synthesized from the same gene in the different 
      organs (liver and oviduct). The carbohydrate composition of yolk-RBP was 
      identical to that of plasma-RBP but different from that of white-RBP showing that 
      the processing of the carbohydrate chains in the liver was different from that in 
      the oviduct.
FAU - Norioka, N
AU  - Norioka N
FAU - Okada, T
AU  - Okada T
FAU - Hamazume, Y
AU  - Hamazume Y
FAU - Mega, T
AU  - Mega T
FAU - Ikenaka, T
AU  - Ikenaka T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Amino Acids)
RN  - 0 (Carbohydrates)
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (riboflavin-binding protein)
RN  - EC 3.4.21.4 (Trypsin)
RN  - OS382OHJ8P (Cyanogen Bromide)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acids/analysis
MH  - Animals
MH  - Carbohydrates/analysis
MH  - Carrier Proteins/analysis/*blood
MH  - Chickens
MH  - Chromatography, High Pressure Liquid
MH  - Cyanogen Bromide
MH  - Egg White/*analysis
MH  - Egg Yolk/*analysis
MH  - Female
MH  - *Membrane Transport Proteins
MH  - Peptide Fragments/analysis
MH  - Trypsin
EDAT- 1985/01/01 00:00
MHDA- 1985/01/01 00:01
CRDT- 1985/01/01 00:00
PHST- 1985/01/01 00:00 [pubmed]
PHST- 1985/01/01 00:01 [medline]
PHST- 1985/01/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a135044 [doi]
PST - ppublish
SO  - J Biochem. 1985 Jan;97(1):19-28. doi: 10.1093/oxfordjournals.jbchem.a135044.