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一种具有冷沉淀性和热沉淀性的单克隆IgA(λ)蛋白的化学和遗传学特征

Chemical and genetic characterization of a monoclonal IgA(lambda) protein with both cryo- and pyro-precipitability.

作者信息

Wang A C, Fudenberg H H, Wang I Y, Watanabe A

出版信息

Scand J Immunol. 1976;5(4):311-6. doi: 10.1111/j.1365-3083.1976.tb00284.x.

Abstract

Studies of a monoclonal IgA (lambda) protein with both cryo- and pyro-precipitability show that it belongs to the IgA2 subclass and is positive for the A2m(2) allotypic marker. Like other cryoglobulins, this protein also has an unblocked light chain, and its heavy chain belongs to the VHI subgroup. The first 22 N-terminal amino acids of the lambda chain of this protein showed less than 65% homology with those of other human lambda chains but showed 86% identity with that of an amyloid fibril protein reported by others. The alpha chain of this protein appears to have more glutamic acid or glutamine, or both, and less isoleucine residues than other human alpha chains.

摘要

对一种具有冷沉淀性和热沉淀性的单克隆IgA(λ)蛋白的研究表明,它属于IgA2亚类,并且对A2m(2)同种异型标记呈阳性。与其他冷球蛋白一样,这种蛋白也具有未封闭的轻链,其重链属于VHI亚组。该蛋白λ链的前22个N端氨基酸与其他人λ链的同源性低于65%,但与其他人报道的一种淀粉样纤维蛋白的同源性为86%。与其他人α链相比,该蛋白的α链似乎含有更多的谷氨酸或谷氨酰胺,或两者皆有,而异亮氨酸残基较少。

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