Abstract
The amino acid sequences of the two major isozymes of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis, were determined by analyzing the tryptic peptides derived from the reduced and carboxymethylated (RCm-) derivative of each isozyme. Amino acid substitutions were shown to occur at eight positions. Rhizopuspepsin I, with an isoelectric point of 5.1, had Ile-15, Asn-61, Ser-116, Lys-162, Ile-230, Tyr-241, Asp-293, and Glu-325, whereas rhizopuspepsin II, with an isoelectric point of 5.8, had Val-15, Lys-61, Asn-116, Ser-162, Val-230, Ser-241, Asn-293, and Gln-325, the other parts of the two isozymes being identical with each other. Thus, rhizopuspepsin I had two more net negative charges than rhizopuspepsin II. This is consistent with the difference in isoelectric point of these two isozymes.
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