Changes in proteins from yolk and in the activity of benzoyl-L-tyrosine ethyl ester hydrolase from the yolk sac membrane during embryonic development of the chicken.
The wet weight and nitrogen content in the water soluble fraction and granule fraction of chicken egg yolk changed during embryonic development. Rapid decreases between Days 14 and 16 were the largest changes observed. When protein components in the soluble and granule fractions of yolk from developing eggs were analyzed by polyacrylamide gel electrophoresis under denaturing conditions, the intensities of bands of some high molecular-weight proteins decreased during incubation, while smaller proteins increased. Most of such changes were observed after Day 16. The activities of proteinases and hydrolases assayed with protein substrates or synthetic substrates at a neutral pH were higher in the yolk sac membrane than in yolk itself. A benzoyl-L-tyrosine ethyl ester hydrolase showed the highest specific activity among the enzymes examined in yolk sac membrane homogenates. Its activity increased after Day 5 of embryogenesis, and became maximum on Days 14 to 20. The data suggest that some of the yolk proteins are degraded by yolk sac membrane enzymes during the latter half of the incubation period.
Sugimoto
Y
Y
Yamada
M
M
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002642:Chick Embryo / Q000502:physiology*; D004527:Egg Proteins / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D013997:Time Factors; D015017:Yolk Sac / Q000201:enzymology*
D004527:Egg Proteins; D002265:Carboxylic Ester Hydrolases; C019780:N-benzoyl-L-tyrosine ethyl ester hydrolase