RtH1 and RtH2, the two hemocyanin isoforms of theprosobranch gastropod Rapana thomasiana, havebeen purified by anion-exchange chromatography andstudied by SDS–PAGE and immunoelectrophoresis.Both subunit types are built up of eight functionalunits (FUs). Under reducing conditions subunit RtH2splits into two fragments, RtH2-a–f and RtH2-gh, suggestingthe presence of a disulfide bridge betweenFU2-f and FU2-g. By proteolytic cleavage of the subunitsinto three-, two-, and single-FU fragments, purificationof fragments by HPLC, N-terminal sequencingof the peptides, and crossed-line immunoelectrophoresis,FUs-a–h of RtH2 and FU-a, FU-d, FU-e, and FU-f ofRtH1 were identified and correlated to the eight-FUspattern of immunoelectrophoresis. FU-a, FU-e, andFU-f of RtH1 and RtH2 are very closely related immunologically.RtH1 and RtH2 both correspond immunologicallyto KLH2, one of the two hemocyanin isoformsof the prosobranch gastropod Megathura crenulata.[...]
Hemocyanin Subunit Organization of the Gastropod Rapana thomasiana
DAINESE, Enrico;
1999-01-01
Abstract
RtH1 and RtH2, the two hemocyanin isoforms of theprosobranch gastropod Rapana thomasiana, havebeen purified by anion-exchange chromatography andstudied by SDS–PAGE and immunoelectrophoresis.Both subunit types are built up of eight functionalunits (FUs). Under reducing conditions subunit RtH2splits into two fragments, RtH2-a–f and RtH2-gh, suggestingthe presence of a disulfide bridge betweenFU2-f and FU2-g. By proteolytic cleavage of the subunitsinto three-, two-, and single-FU fragments, purificationof fragments by HPLC, N-terminal sequencingof the peptides, and crossed-line immunoelectrophoresis,FUs-a–h of RtH2 and FU-a, FU-d, FU-e, and FU-f ofRtH1 were identified and correlated to the eight-FUspattern of immunoelectrophoresis. FU-a, FU-e, andFU-f of RtH1 and RtH2 are very closely related immunologically.RtH1 and RtH2 both correspond immunologicallyto KLH2, one of the two hemocyanin isoformsof the prosobranch gastropod Megathura crenulata.[...]I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.