多种形式的哺乳动物腺苷酸激酶及其抗AK1单克隆抗体。

Enzyme Pub Date : 1990-01-01 DOI:10.1159/000468708
Y Kurokawa, H Takenaka, M Sumida, K Oka, M Hamada, S A Kuby
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引用次数: 6

摘要

研究人员试图确定哺乳动物组织中多种形式腺苷酸激酶(AK)同工酶的细胞内分布,以阐明它们的生理作用,特别是在能量代谢中的作用。等电聚焦获得的腺苷酸激酶酶谱图产生了两种典型的同工型模式:(1)pI大于等于9和8.6,这是牛骨骼肌、心脏、主动脉和大脑的特异性;(2)pI = 7.9和7.1,这是肝脏和肾脏的特异性。模式(1)归因于胞质同工酶(AK1),通过抗AK1免疫染色证实。模式(2)归因于线粒体同工酶(AK2)。这些结果在很大程度上被色谱仪聚焦实验所证实。AK1同工酶部分从牛主动脉平滑肌细胞质中纯化得到,表观Mr为23.5千道尔顿。从比较的角度讨论了其动力学特征。最后,用针对结晶猪肌AK1的单克隆抗体进行Western blotting检测人血清AK1亚型。这些结果为进一步研究杜氏肌营养不良患者血清中异常的腺苷酸激酶同工酶奠定了基础。
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Multiforms of mammalian adenylate kinase and its monoclonal antibody against AK1.

An attempt has been made to determine the intracellular distribution of the multiforms of the adenylate kinase (AK) isoenzymes in mammalian tissues, to shed some light on their physiological roles, especially in energy metabolism. The adenylate kinase zymograms obtained from isoelectric focusing yielded two typical isoform patterns: (1) with a pI greater than or equal to 9 and 8.6, specific for bovine skeletal muscle, heart, aorta and brain, and (2) with a pI = 7.9 and 7.1, specific for liver and kidney. Pattern (1) was attributed to the cytosolic isoenzyme (AK1) as demonstrated by immunostaining with anti-AK1. Pattern (2) was attributed to the mitochondrial isoenzyme (AK2). These results were largely confirmed by chromatofocusing experiments. The AK1 isoenzyme was partially purified from the cytosol fraction of bovine aortic smooth muscle and had an apparent Mr of 23.5 kilodaltons. Its kinetic features are discussed from a comparative standpoint. Finally, the human serum AK1 isoform was also detected by Western blotting with a monoclonal antibody directed against crystalline porcine muscle AK1. These results are to form the basis of further studies on the 'aberrant' adenylate kinase isoenzyme from the serum of Duchenne muscular dystrophics.

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