Abstract
Early in the evolution of the living cell there must have appeared proteins that spanned the plasma membrane and which mediated the uptake and disposal of specific molecules. Proteins of this kind, that were bound to the cell membrane and that were partially exposed to the exterior of the cell, might also have come to serve other functions, such as degrading macromolecules in the surrounding medium to forms that could be taken up and be used as nutrients by the cell. It is reasonable to assume that it would have been an advantage for those early cells to shed, or secrete, those degrading proteins, thereby making the processing of the nutrients in the medium more efficient (1).
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Nygård, O., Westermann, P. (1983). On the Transport of Secretory Proteins From the Endoplasmic Reticulum to the Golgi Complex. In: Abraham, A.K., Eikhom, T.S., Pryme, I.F. (eds) Protein Synthesis. Humana Press. https://doi.org/10.1007/978-1-4612-5310-5_21
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DOI: https://doi.org/10.1007/978-1-4612-5310-5_21
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