Abstract
1. 1. The heterogeneity of α amylases from the hepatopancreas of Palaemon elegans was studied by electrophoresis. Seven forms were detected in polyacrylamide gels in Davis' system. Their mol. wts were between 29,000 and 78,000 as determined by SDS electrophoresis. 2. 2. Purification was performed by affinity chromatography and ion exchange HPLC. Three classes which could be assessed by immunoelectrophoresis were separated. 3. 3. During the intermolt cycle, changes in protein synthesis were shown to be related to changes in the amounts of α amylase variants measured by immunoelectrophoresis. 4. 4. Changes of the α amylase pattern were not reliable to specific activities. Maximum activity was found in post-moult B and pre-moult D 1‴ stages. 5. 5. In vivo activation may explain variations in α amylase activities.
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