A dual role for the Ca2+-requiring proteinase in the degradation of hemoglobin by erythrocyte membrane proteinases.
- 1 November 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (21) , 6714-6717
- https://doi.org/10.1073/pnas.81.21.6714
Abstract
Binding of Hb chains to human erythrocyte membranes is an obligatory step in the conversion of Hb to acid-soluble products by erythrocyte proteinases. This binding requires limited proteolysis of the Hb chains and also modification of the inner surface of the erythrocyte membrane, both of which result from the action of a soluble Ca2+-requiring neutral proteinase. Final digestion of the bound Hb chains in the membrane complex results from the action of intrinsic membrane endopeptidases. Regulation of the activity of the Ca2+-requiring proteinase by the substrate provides a mechanism for the initation of selective protein turnover.This publication has 17 references indexed in Scilit:
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