Characterization of proteins from arthrodial membranes of the lobster, Homarus americanus.
作者： Svend Olav Andersen
DOI: 10.1016/S1095-6433(98)10146-0
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摘要: A total of six proteins from the abdominal arthrodial membrane (intersegmental membrane) lobster, Homarus americanus, were purified and their amino acid sequences determined by a combination mass spectrometry Edman degradation. The are acidic with pI-values close to 4 they all have molecular masses approximately 12 kDa. five differ in only few residues, while sixth protein differs others more than half positions. Only little similarity is observed between those calcified parts exoskeleton H. americanus. contain Rebers-Riddiford consensus sequence common insect cuticles. Comparison complete available databases shows that lobster closely related pliant cuticles derived destined for sclerotization. Characteristic features discussed, it suggested various regions specific roles determining mechanical properties membranes.
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