A comparative study of the structure of egg-white riboflavin binding protein from the domestic fowl and Japanese quail.
作者信息
Walker M, Stevens L, Duncan D, Price N C, Kelly S M
机构信息
Department of Biological and Molecular Sciences, University of Stirling, Scotland, UK.
出版信息
Comp Biochem Physiol B. 1991;100(1):77-81. doi: 10.1016/0305-0491(91)90088-u.
PMID:1756622
Abstract
- 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.
摘要
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