No abstract

The vacuolar-type proton pump ATPase (V-ATPase) plays several pivotal roles in the acidification of diverse intracellular compartments and the extracellular environment. The a subunit isoforms a1, a2, and a3, constituting the membrane-embedded section, are expressed in various tissues, and they are involved in the regulation of subcellular localization and activity of the holocomplex. Therefore, the characterization of their properties is indispensable for dissection of the physiological roles of the V-ATPase in highly differentiated cells. In this study, we report the production and characterization of chicken monoclonal antibodies (MAbs) against these mouse a1, a2 and a3 subunit isoforms. These MAbs are shown to be suitable for both immunoblotting and immunofluorescence analysis. The MAbs obtained in this study are useful in understanding the pathological basis of V-ATPase dysfunction.

In the pond-culture of prawn, Penaeus japonicus, the soft part of short-necked clam, Tapes japonica, is commonly used as a sole diet and it has been observed that the prawns are attracted intensely by its press-juice".As a preliminary study for the exploitation of artificial feed mixture, the extracts of the soft part were analyzed for various components in order to identify the attractant and the amino acid composition of its protein was examined.Hot-water extracts of the homogenized soft part were made to 70% (v/v) concentration of EtOH, and organic acids, nucleotides and their related compounds, the amounts of quaternary ammonium bases and free amino acids before and after hydrolysis were determined on the supernatant.The precipitates were subjected to the determination of glycogen. The residues from hotwater extraction were applied to the analysis of amino acid composition of the protein.Results obtained are summarized as follows.