Protein pattern variability of the hemolymph of mantis shrimp, Squilla mantis L. (crustacea, stomatopoda)

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Abstract
The SDS‐PAGE of Squilla mantis hemolymph reveals 16 major protein bands. Three of them, showing a molecular weight (MW) around 125 kdal, are female specific proteins (FSP) to be considered as vitellogenins because their amount increases with ovarian maturity. The MW of the hemocyanin subunit is confirmed around 70 kdal. Low MW proteins appear or intensify at molt. Hemolymph incubation with 35S‐Methionine and subsequent autoradiography of SDS‐PAGE slabs show that hemocyanin and vitellogenins are not synthesized by the circulating hemocytes, while some proteins connected with molt are heavily labeled by the tracer.