Morrison S L, Scharff M D
Eur J Immunol. 1979 Jun;9(6):461-5. doi: 10.1002/eji.1830090609.
A spontaneous assembly variant, B 50, has been isolated from the MPC-11 mouse myeloma cell line. This variant synthesizes fewer light chains per cell than the parent resulting the production of a slight molar excess of heavy chains. These changes are associated with a delay and change in the pathway of assembly and a delay in secretion. Spontaneous revertants of B 50 have been obtained, all of which synthesize normal amounts of light chains and assemble and secrete the immunoglobulin molecule through the same pathways and with the same kinetics as the parental cells. A comparison of the tryptic-chymotryptic peptides of the parental, variant and revertant heavy and light chains did not reveal any differences. These studies indicate that variants in mouse myeloma cells can arise with defects in the quantitative expression of the immunoglobulin gene and suggest that the presence of excess light chains facilitates the assembly and secretion of some immunoglobulin molecules.
从MPC - 11小鼠骨髓瘤细胞系中分离出一种自发组装变体B 50。该变体每个细胞合成的轻链比亲本少,导致重链在摩尔数上略有过量。这些变化与组装途径的延迟和改变以及分泌延迟有关。已获得B 50的自发回复突变体,所有回复突变体合成的轻链量正常,并通过与亲本细胞相同的途径和相同的动力学组装和分泌免疫球蛋白分子。对亲本、变体和回复突变体重链和轻链的胰蛋白酶 - 糜蛋白酶肽段进行比较,未发现任何差异。这些研究表明,小鼠骨髓瘤细胞中的变体可能因免疫球蛋白基因定量表达缺陷而产生,并表明过量轻链的存在有助于某些免疫球蛋白分子的组装和分泌。