Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Studies on Egg White Protein
Heterogeneity of Ovomucoid
Masao KANAMORIMakoto KAWABATA
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1969 Volume 33 Issue 1 Pages 75-79

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Abstract
The carbohydrate of ovomucoid was analyzed for components I, II, III and IV which were. fractionated by CMC-column chromatography. The total hexose content and the molar ratio of D-mannose to D-galactose (4:1) were identical in each component, but the D-glucosamine and sialic acid contents were found to be higher in components I and II (both are trypsin inhibitors) compared with components III and IV (both are apo-proteins of flavomucoid). The amino acid composition of each component of ovomucoid varied considerably. There were remarkable differences in the amino acid composition between components I and II, both had an antitryptic activity. The N-terminal amino acid of components I and II was alanine and in the case of components III and IV, threonine was found on the N-terminal. The free carboxylic residue of sialic acid was found to be responsible for the negative charge of ovomucoid, and its electrophoretic heterogeneity was reaffirmed by paper electrophoresis. It is evident from the ultracentrifugal analysis that the four components of ovomucoid have a similar molecular size.
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