The core polypeptide components of the intact phycobilisomes (PBSs) prepared by the sucrose gradients in 0.9 M phosphate buffer from a thermophilic cyanobacterium Myxosarcina concinna Printz were investigated. Three allophycocyanins, designated AP1, AP2, and AP3, of the PBS cores were successfully prepared by using the gradient polyacrylamide gel electrophoresis (PAGE) performed in neutral, instead of alkaline, buffer system. The spectral properties of AP2 and AP3 demonstrated that they both had fluorescence emission maxima at 684/685 nm at 77 K, which was identical to those of the intact PBSs, and showed the absorption of allophycocyanin B (AP-B) subunit. Sodium dodecyl sulfate-PAGE revealed that the three biliprotein complexes were all composed of heterogeneous subunits and two more linker polypeptides (Ls), AP1 alpha(22.3)alpha(19.5)beta(17.4)beta(15.7)L(13.8)L(11.3)L(9.5), AP2 alpha(22.3)alpha(19.5)beta(17.4)beta(15.7)beta(15.1)L(11.3)L(9.5), and AP3 alpha(22.3)alpha(19.5)beta(17.4)beta(15.7)beta(15.1)L(11.3)L(9.5)L(8.3). Compared with the characteristics of AP1, beta(15.1), which belonged to the beta subunit group, was the AP-B subunit of AP2 and AP3. Because AP2 was only obtained together with the PBS by the aid of 2% (v/v) Triton X-100, but not AP3, it was closely related to anchoring the PBS core on thylakoid membranes though the polypeptide analysis showed that AP2 had no core-membrane linker (LCM). Aggregates of the three AP biliproteins were proposed based on the present results, and their functions in the PBS core construction and the energy transfer to PS II and PS I were discussed.