Hubert M, Barin F, Goudeau A
J Virol Methods. 1982 Jan;3(6):349-54. doi: 10.1016/0166-0934(82)90039-8.
Purified hepatitis B surface antigen (HBsAg) of subtype ay was solubilized in guanidinium chloride and submitted to chromatography on Sepharose 4B in the presence of guanidinium chloride. The polypeptides P1 (Mr = 24,000) and P2 (Mr = 29,000) were eluted in the same fraction with a minor contaminant (Mr = 40,000). Large amounts of these two polypeptides were obtained in a single step. This technique which constitutes a method for large-scale purification of the P1 and P2 polypeptides should permit more complete characterization of the P1 and P2 polypeptides and of their antigenic determinants.
ay亚型的纯化乙型肝炎表面抗原(HBsAg)溶解于氯化胍中,并在氯化胍存在的条件下在琼脂糖4B上进行层析。多肽P1(Mr = 24,000)和P2(Mr = 29,000)与一种少量污染物(Mr = 40,000)在同一级分中被洗脱。一步就获得了大量的这两种多肽。这种构成大规模纯化P1和P2多肽方法的技术应该能使对P1和P2多肽及其抗原决定簇进行更全面的表征成为可能。