牛心F1 ATP酶上的腺嘌呤核苷酸结合位点：β亚基非催化位点的酪氨酸-368和催化位点的β酪氨酸-345的光亲和标记
Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.
作者信息
Cross R L, Cunningham D, Miller C G, Xue Z X, Zhou J M, Boyer P D
出版信息
Proc Natl Acad Sci U S A. 1987 Aug;84(16):5715-9. doi: 10.1073/pnas.84.16.5715.
Abstract
2-Azidoadenine [32P]nucleotide was bound specifically at catalytic or noncatalytic nucleotide binding sites on beef heart mitochondrial F1 ATPase. In both cases, photolysis resulted in nearly exclusive labeling of the beta subunit. The modified enzyme was digested with trypsin, and labeled peptides were purified by reversed-phase high-pressure liquid chromatography. Amino acid sequence analysis of the major 32P-labeled tryptic fragments showed beta-subunit Tyr-368 to be present at noncatalytic sites and beta Tyr-345 to be present at catalytic sites. From the relationship between the degree of inhibition and extent of modification, it is estimated that one-third of the catalytic sites or two-thirds of the noncatalytic sites must be modified to give near-complete inhibition of catalytic activity.
摘要
2-叠氮腺嘌呤[32P]核苷酸特异性结合于牛心线粒体F1 ATP酶的催化或非催化核苷酸结合位点。在这两种情况下，光解几乎专一性地标记了β亚基。用胰蛋白酶消化修饰后的酶，通过反相高压液相色谱法纯化标记的肽段。对主要的32P标记胰蛋白酶片段进行氨基酸序列分析，结果表明β亚基Tyr-368存在于非催化位点，β Tyr-345存在于催化位点。根据抑制程度与修饰程度之间的关系估计，必须修饰三分之一的催化位点或三分之二的非催化位点才能几乎完全抑制催化活性。
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