Evidence of homing of black rockfish Sebastes inermis using biotelemetry

ABSTRACT: The black rockfish Sebastes inermis is one of the most important fishery species along the coast from southern Hokkaido to Kyushu, Japan and is often found in rocks and Zostera areas. We conducted biotelemetry using coded ultrasonic transmitters to clarify the movement of the black rockfish that inhabited the seawall of the Kansai International Airport. We released 25 black rockfish at two points. One was the airport seawall and the other was side shallows off the Sensyu district. Seventeen black rockfish returned to their capture site after release. We used the V -test to determine whether the direction of movement was random or orientated. The black rockfish moved at random along the seawall within some hours after release ( P  > 0.05). Four hours after release, they moved to their home site intentionally ( P  < 0.0025).     

Expression of a recombinant crustacean hyperglycemic hormone of the kuruma prawn Penaeus japonicus in methylotrophic yeast Pichia pastoris

ABSTRACT:   Until now, six crustacean hyperglycemic hormones (CHH) designated Pej-SGP-I, -II, -III, -V, -VI and -VII have been characterized in the kuruma prawn Penaeus japonicus . All CHH consist of 72 amino acid residues and have an amidated carboxyl (C)-terminus. In the present study, we expressed Pej-SGP-III in methylotrophic yeast Pichia pastoris in order to obtain a large quantity of recombinant CHH possessing biological activity. A cDNA encoding Pej-SGP-III that had been previously cloned was processed by polymerase chain reaction (PCR) and the resulting product was ligated into an expression vector. Pichia pastoris was transformed with this vector after which a recombinant Pej-SGP-III was expressed having an additional amino acid residue (glycine) at the C-terminus (rPej-SGP-III-Gly), a form considered to be a putative precursor of this hormone. rPej-SGP-III-Gly secreted into the culture medium was purified by reversed-phase HPLC, and amidated using a peptidylglycine alpha-amidating enzyme. The amidated rPej-SGP-III (rPej-SGP-III) showed hyperglycemic activity in in vivo bioassay almost comparable to that of the natural Pej-SGP-III. rPej-SGP-III thus obtained will be a useful tool not only for its physiological study but also for the determination of its 3-D structure.