| Popis: |
1. 1. Two dimensional electrophoresis (IEF-SDS) of the spider crab Acanthonyx lunulatus hemolymph shows the presence of four polypeptide AL1 (molecular weight 74,000), AL2 (76,000), AL3 (81,000) and AL4 (84,000). This method allows a rapid and reproducible characterization of hemolymph proteins. 2. 2. When hemocyanin is purified by high speed centrifugations the resulting pellet contains the same four polypeptides showing that hemocyanin is the major component of the hemolymph of Acanthonyx lunulatus. 3. 3. Qualitative changes in hemolymph protein associated with molting has been demonstrated by IEF-SDS: a new polypeptide AL5 (88,000) different from protein AL1, AL2, AL3 and AL4 (as shown by the limited proteolysis technique of Cleveland, 1977) is present at stages D0, D1, D2 D3. This protein appears in hemolymph when the ecdysone titer increases. |
