Abstract
Mammalian aspartic proteinases are synthesized as inactive precursors or zymogens. Stomach zymogens undergo a conversion to the active enzyme form autocatalytically at pH < 5.0 (1). The human gastric juice has two major groups of aspartic proteinases, the pepsins (EC3.4.23.1) and the gastricsins (EC3.4.23.3). Progastricsin or pepsinogen C (PGC) is converted to gastricsin by removal of the 43 amino-terminal residues of the prosegment. The resulting mature gastricsin has 329 amino acid residues. The sequence of human PGC has been determined independently in two laboratories by nucleotide sequencing of the gene (2) and of cDNA clones (3).
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Tarasova, N., James, M., Moore, S., Sielecki, A., Chernaia, M. (1995). The Molecular Structure of Human Progastricsin and its Comparison with that of Porcine Pepsinogen. In: Takahashi, K. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 362. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1871-6_2
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DOI: https://doi.org/10.1007/978-1-4615-1871-6_2
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