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血红蛋白特伦托:由于一种新的移码突变[β144(-A)]导致β链C末端延长。

Hb Trento: an elongated C-terminal beta chain due to a new frameshift mutation [beta144 (-A)].

作者信息

Ivaldi Giovanni, David Onorata, Baffico Maria, Leone Daniela, Baldi Maurizia, Parodi Maria Isola, Scimè-Degani Valeria, Piga Antonio, Scagni Paola, Rabino-Massa Emma, Ricco Giuseppe

机构信息

Laboratorio Genetica Umana, Ospedali Galliera, Genova, Italia.

出版信息

Hemoglobin. 2003 Feb;27(1):15-25. doi: 10.1081/hem-120018432.

Abstract

An elongated C-terminal hemoglobin variant, due to the deletion of nucleotide A in codon 144 (nucleotide 63600 GenBank entry UO1317) was found in a 31-year-old woman from Trento (northeastern Italy). This deletion led to the replacement of lysine at beta144 by a serine residue, the disappearance of the stop codon at position 147, and the presence of 12 additional residues, identical to those observed in Hbs Saveme, Tak and Cranston, which result from a similar mechanism. Hb Trento, amounting to 29% of the total hemoglobin, was unstable and had, as the other variants of this group, an increased oxygen affinity. It led to a mild compensated hemolytic anemia with red cell inclusion bodies. Functional studies of the isolated abnormal hemoglobin were difficult to perform because of autoxidation, precipitation, and formation of hybrids with Hb A.

摘要

在一名来自意大利东北部特伦托的31岁女性中发现了一种延长的C末端血红蛋白变体,这是由于密码子144(GenBank登录号UO1317的核苷酸63600)中的核苷酸A缺失所致。这种缺失导致β144位的赖氨酸被丝氨酸残基取代,147位的终止密码子消失,并出现了另外12个残基,与在Hbs Saveme、Tak和Cranston中观察到的残基相同,这些都是由类似机制导致的。特伦托血红蛋白(Hb Trento)占总血红蛋白的29%,不稳定,与该组的其他变体一样,具有增加的氧亲和力。它导致了轻度代偿性溶血性贫血,并伴有红细胞包涵体。由于自氧化、沉淀以及与Hb A形成杂种,对分离出的异常血红蛋白进行功能研究很困难。

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