Proteolytic enzymes in yolk-sac membrane of quail egg. Purification and enzymatic characterisation

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
B GerhartzJ Wittmann

Abstract

Degradation of yolk protein is essential for the early development of the avian embryo. In Japanese quail (Coturnix coturnix japonica), proteolysis in the surrounding tissue of the yolk, the yolk-sac membrane, can be inhibited by class-specific inhibitors of cysteine proteinases as well as of aspartic proteinases. Purification of the enzymes leads to one cysteine proteinase and one aspartic proteinase with an apparent molecular mass of 29 kD and 44 kD, respectively. Both enzymes were purified in a two-chain form, although a single-chain form is also present in the homogenate of yolk-sac membrane. The cysteine proteinase was identified by NH2-terminal sequence analysis as well as by kinetic studies as a new cathepsin B from quail. Like mammalian cathepsin B, this avian cathepsin B exhibits two different kinds of proteolytic activity, an endopeptidase activity and a dipeptidyl carboxypeptidase activity. Chicken egg white cystatin, a protein-aceous cysteine proteinase inhibitor, inhibits quail cathepsin B with an equilibrium dissociation constant (Ki) of 3.3 nM. Likewise the aspartic proteinase was identified as a new cathepsin D from quail. This avian cathepsin D has a different processing site to all known mammalian cathepsins D...Continue Reading

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Citations

Jul 30, 1999·Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology·B GerhartzJ Wittmann
May 14, 2008·Journal of Experimental Zoology. Part B, Molecular and Developmental Evolution·Richard P Elinson
Jan 10, 2018·Journal of Experimental Zoology. Part B, Molecular and Developmental Evolution·Seba Jamal Shbailat, Ibtisam Omar Aslan
Feb 2, 2021·Poultry Science·E A Wong, Z Uni
Jun 30, 2009·The Journal of Experimental Biology·Guojin Wu, Zandong Li

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