Gaĭnutdinov M Kh, Ishmukhamedov R N, Konov V, Luchenko M B, Mirmakhmudova S
Biokhimiia. 1988 Feb;53(2):196-204.
A thermostable low molecular weight glycopeptide containing syalic acids, which uncouples mitochondrial oxidative phosphorylation, has been detected, isolated and purified from rat liver cytoplasm. In the presence of the glycopeptide, oxidative phosphorylation in rat liver mitochondria is uncoupled by low physiological concentrations of Ca2+, which otherwise do not have any appreciable effect on the mitochondria. Oxidative phosphorylation uncoupling by the glycopeptide is accompanied by an increase of the mitochondrial volume. This process has a limited amplitude and is regulated by changes in Ca2+ concentration in the extramitochondrial space. The glycopeptide has been shown to induce K+ transport across the inner mitochondrial membrane, this effect is enhanced by Ca2+.
一种含有唾液酸的热稳定低分子量糖肽已从大鼠肝脏细胞质中被检测、分离和纯化出来,它能使线粒体氧化磷酸化解偶联。在该糖肽存在的情况下,大鼠肝脏线粒体中的氧化磷酸化会被低生理浓度的Ca2+解偶联,而Ca2+在其他情况下对线粒体没有明显影响。糖肽导致的氧化磷酸化解偶联伴随着线粒体体积的增加。这个过程幅度有限,并受线粒体外空间Ca2+浓度变化的调节。已证明该糖肽能诱导K+跨线粒体内膜运输,Ca2+可增强这种作用。