Caulin-Glaser T, Prelli F, Franklin E C
J Lab Clin Med. 1982 Jun;99(6):845-51.
An IgM-lambda pyroglobulin from a patient with Waldenström's syndrome was studied. Heavy and light chains were separated and their N-terminal amino acid sequence determined. The heavy chain was unblocked and belonged to the VHIII subclass, and the light chain belonged to the lambda I subclass. Factors influencing pyroprecipitability were examined through experiments designed to study some of the physical and chemical properties of an IgM-lambda pyroglobulin. Pyroprecipitability was affected by pH, ionic strength, urea, and reducing agents, suggesting an involvement of noncovalent electrostatic interactions. It was also demonstrated through recombinant experiments that it is necessary to have covalently joined homologous heavy and light chains in pentameric form for pyroprecipitation to occur. Since neither heavy nor light chains had any unique structural features, the reasons for this property remain obscure but may reflect the result of conformational factors.
对一名患有瓦尔登斯特伦巨球蛋白血症患者的IgM-λ热沉淀球蛋白进行了研究。分离出重链和轻链,并测定了它们的N端氨基酸序列。重链未被封闭,属于VHIII亚类,轻链属于λI亚类。通过旨在研究IgM-λ热沉淀球蛋白某些物理和化学性质的实验,研究了影响热沉淀性的因素。热沉淀性受pH值、离子强度、尿素和还原剂的影响,表明非共价静电相互作用参与其中。重组实验还表明,五聚体形式的同源重链和轻链必须共价连接才能发生热沉淀。由于重链和轻链都没有任何独特的结构特征,这种性质的原因仍然不清楚,但可能反映了构象因素的结果。