血红蛋白M奥尔登堡被鉴定为α2亚基第87位（F8）的组氨酸被β2亚基的酪氨酸所取代。
Hemoglobin M Oldenburg identified as HB alpha 2 87(F8)His replaced by Tyr beta 2.
作者信息
Steffens G, Steffens G, Buse G
出版信息
Hoppe Seylers Z Physiol Chem. 1977 Jan;358(1):35-8. doi: 10.1515/bchm2.1977.358.1.35.
The abnormal hemoblobin designated as Hb M Oldenburg and already characterized as alpha 2 (72,87 or 89)His replaced by Tyr beta 2 was further identified by isolation, amino acid analysis and automated sequencing of the altered tryptic peptide alpha TIX. In this peptide the histidine in the position 87 is replaced by a tyrosine reside. Thus Hb M Oldenburg has to be described as alpha 2 87(F8)His replaced by Tyr beta 2 and is, therefore, identical with the mutant hemoblobins M Iwate and M Kankakee.
被命名为Hb M奥尔登堡的异常血红蛋白，已被鉴定为α2（72、87或89位）组氨酸被β2位酪氨酸取代，通过对改变后的胰蛋白酶肽αTIX进行分离、氨基酸分析和自动测序进一步得到确认。在该肽段中，87位的组氨酸被一个酪氨酸残基取代。因此，Hb M奥尔登堡必须被描述为α2 87（F8）组氨酸被β2位酪氨酸取代，所以它与突变血红蛋白M岩手和M坎卡基相同。
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