血红蛋白被一种长链交联剂：癸二酸双（3,5-二溴水杨酸酯）修饰。

The modification of hemoglobin by a long crosslinking reagent: bis(3,5-dibromosalicyl) sebacate.

作者信息

Zhang Q, Olsen K W

机构信息

Department of Chemistry Loyola University of Chicago, IL 60626.

出版信息

Biochem Biophys Res Commun. 1994 Sep 30;203(3):1463-70. doi: 10.1006/bbrc.1994.2349.

DOI:10.1006/bbrc.1994.2349

PMID:7945292

Abstract

Bis(3,5-dibromosalicyl) sebacate is a bifunctional protein crosslinking reagent. It reacts with oxy form of human hemoglobin A to produce a crosslinked hemoglobin between two beta chains in the 2,3-bisphosphoglycerate binding cleft, decreasing the oxygen affinity. The oxygen binding curve of crosslinked hemoglobin had a P50 of 18.5 mmHg compared to a P50 of 11.0 mmHg for native hemoglobin and remains highly cooperative, n = 2.2. Crosslinking hemoglobin between the two beta chains also results in a 12.5 degrees C increase in the thermal denaturation temperature. The crosslinked hemoglobin is oxidized more rapidly to methemoglobin. Its autoxidation rate in 0.01 M MOPS, pH 7.4, at 37 degrees C was 1.4 times as fast as that of Hb A.

摘要

癸二酸双（3,5-二溴水杨酸）酯是一种双功能蛋白质交联剂。它与人血红蛋白A的氧合形式反应，在2,3-二磷酸甘油酸结合裂隙处的两条β链之间产生交联血红蛋白，降低氧亲和力。交联血红蛋白的氧结合曲线的P50为18.5 mmHg，而天然血红蛋白的P50为11.0 mmHg，并且仍具有高度协同性，n = 2.2。两条β链之间的血红蛋白交联还导致热变性温度升高12.5℃。交联血红蛋白被氧化为高铁血红蛋白的速度更快。在37℃、pH 7.4的0.01 M MOPS中，其自动氧化速率是Hb A的1.4倍。