Garbarz M, Devaux I, Grandchamp B, Picat C, Dhermy D, Lecomte M C, Boivin P, Sahr K E, Forget B
I.N.S.E.R.M., Unité n. 160, Hôpital Beaujon, Clichy.
C R Acad Sci III. 1989;308(2):43-8.
We have undertaken to identify the spectrin gene mutation in a patient with a severe hemolytic form of Hereditary Elliptocytosis with homozygosity for the spectrin alpha I/74 variant. This variant corresponds to the presence of a 74,000 peptide which is produced during mild tryptic digestion of spectrin by cleavage at the Arginine-39 of the alpha I/80,000 domain of the spectrin alpha chain (595 amino acids). We hypothesized that the alpha I/74 mutation would be closed to the cleavage site Arg-39. A genomic library built with the patient's DNA was screened with a probe corresponding to a fragment of the alpha spectrin gene. Two clones were isolated, one being of paternal, the other of maternal origin. The subclones obtained contained the alpha spectrin gene exons 2 and 3 which encode for the first 88 amino-acids of the spectrin alpha I domain. The sequences obtained did not show any abnormality. The implications of these results are discussed.
我们已着手鉴定一名患有严重溶血性遗传性椭圆形红细胞增多症患者的血影蛋白基因突变情况,该患者血影蛋白αI/74变体呈纯合状态。此变体对应一种74,000肽的存在,该肽是在血影蛋白经胰蛋白酶轻度消化时,通过血影蛋白α链αI/80,000结构域(595个氨基酸)的精氨酸-39处裂解产生的。我们推测αI/74突变可能靠近裂解位点精氨酸-39。用与α血影蛋白基因片段对应的探针筛选了用患者DNA构建的基因组文库。分离出两个克隆,一个来自父本,另一个来自母本。获得的亚克隆包含血影蛋白αI结构域前88个氨基酸编码的血影蛋白α基因外显子2和3。所得序列未显示任何异常。讨论了这些结果的意义。