Abstract
1. 1. Hemocyanin from the spiny lobster Palinurus vulgaris was separated into two fractions, which were designated as subunits a and b. 2. 2. 55% of the amino acid sequence of subunit b has been determined. A comparison with Panulirus interruptus hemocyanins shows 78% sequence identity with subunit a and 56% with subunit c. It has carbohydrate attached to domain. Two half-cystines have been substituted, indicating that it probably possesses only one disulfide bridge. Heterogeneity has been observed in seven out of 380 positions determined so far. 3. 3. Subunit a is almost identical with subunit b. In contrast to Panulirus interruptus and Panulirus japonicus, Palinurus vulgaris hemocyanin contains no c-type subunit. 4. 4. A position in the tentative evolutionary tree of arthropod hemocyanins based on sequence differences has been assigned to Palinurus vulgaris subunit b.
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