The Globin Composition of Daphnia pulex Hemoglobin
Although the majority of Crustacea have He as an O2 carrier, extracellular Hbs are mainly found in the hemolymph of the Branchiopoda. Basing our analysis on globin structure and using Vinogradov’s classification, we may distinguish two groups: the multi-domain-multisubunit Hbs found in Anostraca, and the two domain-multisubunit Hbs found in Notostraca, Conchostraca and Cladocera (1). The Hb of Daphnia pulex is a representative of the latter. It has an S 20°,w of 16.4–16.9, an M r of 420,000–470,000, contains one mole heme per M r = 18,000–20,000, and is composed of different globin chains with M r = 31,000–37,000. Limited proteolysis suggests that one globin chain is comprised of two heme-containing O2 binding domains with M r = 17,000 (2). In this work we describe the globin composition of the D. pulex Hb.
KeywordsHydrolysis Phenol Urea Acetonitrile Glycine
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