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As a final step in the elucidation of the primary structure of subunit a of
Panulirus interruptus hemocyanin (657 residues, Mr 75696 excluding two copper
ions and carbohydrate), the amino acid sequence of the largest fragment obtained
by limited trypsinolysis was determined. The elucidation of the sequence of
residues 176-657, comprising domains two and three, was mainly based on two
digests, with CNBr and trypsin, respectively, from both of which a complete set
of peptides was obtained. Additional sequence information was obtained from a
digest with Staphylococcus aureus V8 protease and from one fragment obtained by
cleaving subunit a with hydroxylamine. A block during Edman degradations
indicated an Asn-Gly sequence at positions 597-598, although only aspartic acid
was identified at position 597.
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