ABSTRACT
The cellular retinol-binding proteins with the molecular weight of 14 and 53.5 kDa have been isolated from the intermediate zone mucosa cells of the glandular stomach in chickens. No substantial differences in the amino acid composition of the investigated proteins have been found. The possible functional role of the isolated cellular retinol-binding proteins is discussed.
Subject(s)
Gastric Mucosa/metabolism , Retinol-Binding Proteins/metabolism , Stomach, Avian/metabolism , Amino Acids/analysis , Animals , Chickens , Chromatography, DEAE-Cellulose , Electrophoresis, Polyacrylamide Gel , Gastric Mucosa/cytology , Molecular Weight , Retinol-Binding Proteins/isolation & purification , Spectrometry, Fluorescence , Spectrophotometry, UltravioletABSTRACT
Glycolipoconjugates of mucin from the intermediate zone of the hen glandular stomach is shown to include at least 5 glycolipoprotein threads with equal molecular weight of about 10 kD but with different lipid content and amino acid composition. Retinol is bound only to 2-3 glycolipoproteins which contain the highest quantity of covalently bound lipids. The retinol-binding with mucin glycolipoprotein threads, probably, occurs like the lipid-lipid interaction; neutral carbohydrates do not participate in this process.