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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(More)
Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many highly conserved residues and extensive regions of near identity. This correspondence can be matched closely(More)
Limited proteolysis of the native monomeric 94-kDa subunit of Panulirus interruptus hemocyanin by trypsin, plasmin and subtilisin produces an 18-kDa fragment, a 71-kDa fragment and a small glycopeptide. In the plasmin digest a 23-kDa precursor of the 18-kDa fragment has been observed. Automatic Edman degradations demonstrated that the 18-kDa fragments have(More)
The amino acid sequence of the first domain (positions 1-175) of Panulirus interruptus hemocyanin subunit a has been determined. The sequence of residues 1-158 (18-kDa fragment obtained by limited proteolysis) was derived from peptides obtained by digestion of this fragment with CNBr and trypsin and by subdigestion of these peptides with other enzymes. The(More)
Incubation of beta-endorphin with cytosolic and particulate fractions of rat brain resulted in the formation of several peptides, including gamma-endorphin [beta-endorphin-(1-17)] and beta-endorphin-(18-31), indicating the presence of enzyme activity cleaving the Leu17-Phe18 bond of beta-endorphin. An assay for this Leu-Phe cleaving activity, based on the(More)
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