Abstract
The primary structure of subunit b of Panulirus interruptus hemocyanin has been derived from two digests (trypsin and CNBr) and, in some cases, with aid from the similarity with the sequence of subunit a. Differences between the amidation states of Asx and Glx residues in subunit b relative to a were investigated more thoroughly. When compared to the sequence of subunit a, 18 differences (2.7%) were found and certain heterogeneities, indicating the presence of a minor subunit b', were observed. Several differences in properties between subunits a and b, including their anomalous behaviour on SDS/polyacrylamide gel electrophoresis, could be explained by amino acid replacements.
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