A comparative study of the structure of egg-white riboflavin binding protein from the domestic fowl and Japanese quail.
1. The riboflavin binding proteins from domestic fowl and Japanese quail have been isolated and their structures compared by circular dichroism, fluorescence and peptide mapping. 2. The two proteins have similar secondary structures, but differ in their tertiary structures as reflected in the environments of aromatic amino acid side chains. 3. Differences in amino acid sequence between the proteins are indicated by the digestion patterns obtained with thermolysin, chymotrypsin and V8 proteinase from Staphylococcus aureus. Both proteins are resistant to digestion by trypsin.
Walker
M
M
Department of Biological and Molecular Sciences, University of Stirling, Scotland, UK.
Stevens
L
L
Duncan
D
D
Price
N C
NC
Kelly
S M
SM
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002645:Chickens; D002942:Circular Dichroism; D003370:Coturnix; D004527:Egg Proteins / Q000737:chemistry* / Q000302:isolation & purification; D005260:Female; D026901:Membrane Transport Proteins; D015394:Molecular Structure; D008970:Molecular Weight; D010449:Peptide Mapping; D012256:Riboflavin / Q000378:metabolism*; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis; D014443:Tyrosine / Q000032:analysis
D002352:Carrier Proteins; D004527:Egg Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D014443:Tyrosine; D014364:Tryptophan; D012256:Riboflavin