Abstract
Human pepsin A was shown to consist of up to four isoforms with differing enzymatic properties [1, 2, 3]. Unfortunately, the absence of complete sequences has hindered progress to any clear explanation for these differences. The sequence data available has been based mainly on N-terminal amino-acid and cDNA analysis of human pepsinogens [2, 4, 5]. We have therefore undertaken further more detailed amino-acid sequence studies of isolated human pepsin isoforms in order to clarify the structural basis for the differences observed in enzymatic activities.
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Tarasova, N. et al. (1995). A Comparative Study on Amino Acid Sequences of Three Major Isoforms of Human Pepsin A. 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_8
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DOI: https://doi.org/10.1007/978-1-4615-1871-6_8
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