{"title":"一价阳离子对超声红细胞膜腺苷三磷酸酶的影响","authors":"Amir Askari, Joseph C. Fratantoni","doi":"10.1016/0926-6569(64)90277-9","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Human erythrocyte membrane contains a Mg<sup>2+</sup>-dependent adenosinetriphosphatase activity. The enhancement of this activity requires the simultaneous presence of Na<sup>+</sup> and K<sup>+</sup>. When the membranes were broken by ultrasonic vibrations, the adenosinetriphosphatase activity was enhanced with either Na<sup>+</sup> and K<sup>+</sup>, and in this case enhancement was no longer affected by ouabain.</p></span></li><li><span>2.</span><span><p>2. The effects of Mg<sup>2+</sup>, Ca<sup>2+</sup>, pH, and detergents on the various manifestations of the adenosinetriphosphatase activity, namely: (a) the Na<sup>+</sup>-plus-K<sup>+</sup>-dependent form, (b) the single-ion-dependent form, and (c) the ion-independent form, were studied. The results did not suggest the presence of more than one enzyme.</p></span></li><li><span>3.</span><span><p>3. Since the single-ion-dependent adenosinetriphosphatase activity was revealed merely by a physical change in the method of preparation (sonication), it is reasonable to suspect that it and the Na<sup>+</sup>-plus-K<sup>+</sup>-dependent activity are different manifestations of a single enzymic activity.</p></span></li></ul></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 132-141"},"PeriodicalIF":0.0000,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90277-9","citationCount":"24","resultStr":"{\"title\":\"Effect of monovalent cations on the adenosinetriphosphatase of sonicated erythrocyte membrane\",\"authors\":\"Amir Askari, Joseph C. Fratantoni\",\"doi\":\"10.1016/0926-6569(64)90277-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Human erythrocyte membrane contains a Mg<sup>2+</sup>-dependent adenosinetriphosphatase activity. The enhancement of this activity requires the simultaneous presence of Na<sup>+</sup> and K<sup>+</sup>. When the membranes were broken by ultrasonic vibrations, the adenosinetriphosphatase activity was enhanced with either Na<sup>+</sup> and K<sup>+</sup>, and in this case enhancement was no longer affected by ouabain.</p></span></li><li><span>2.</span><span><p>2. The effects of Mg<sup>2+</sup>, Ca<sup>2+</sup>, pH, and detergents on the various manifestations of the adenosinetriphosphatase activity, namely: (a) the Na<sup>+</sup>-plus-K<sup>+</sup>-dependent form, (b) the single-ion-dependent form, and (c) the ion-independent form, were studied. The results did not suggest the presence of more than one enzyme.</p></span></li><li><span>3.</span><span><p>3. Since the single-ion-dependent adenosinetriphosphatase activity was revealed merely by a physical change in the method of preparation (sonication), it is reasonable to suspect that it and the Na<sup>+</sup>-plus-K<sup>+</sup>-dependent activity are different manifestations of a single enzymic activity.</p></span></li></ul></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 1\",\"pages\":\"Pages 132-141\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90277-9\",\"citationCount\":\"24\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964902779\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964902779","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 24
摘要
1.1. 人红细胞膜含有Mg2+依赖性腺苷三磷酸酶活性。这种活性的增强需要Na+和K+的同时存在。当超声振动破膜时，Na+和K+都能增强腺苷三磷酸酶的活性，在这种情况下，瓦卡因不再影响增强。2.2。研究了Mg2+， Ca2+， pH和洗涤剂对腺苷三磷酸酶活性的各种表现形式的影响，即:(a) Na+ + k +依赖形式，(b)单离子依赖形式和(c)离子独立形式。结果不表明存在一种以上的酶。由于单离子依赖性腺苷三磷酸酶活性仅通过制备方法的物理变化(超声)显示，因此有理由怀疑它与Na+ + k +依赖性活性是单一酶活性的不同表现。
Effect of monovalent cations on the adenosinetriphosphatase of sonicated erythrocyte membrane
1.
1. Human erythrocyte membrane contains a Mg2+-dependent adenosinetriphosphatase activity. The enhancement of this activity requires the simultaneous presence of Na+ and K+. When the membranes were broken by ultrasonic vibrations, the adenosinetriphosphatase activity was enhanced with either Na+ and K+, and in this case enhancement was no longer affected by ouabain.
2.
2. The effects of Mg2+, Ca2+, pH, and detergents on the various manifestations of the adenosinetriphosphatase activity, namely: (a) the Na+-plus-K+-dependent form, (b) the single-ion-dependent form, and (c) the ion-independent form, were studied. The results did not suggest the presence of more than one enzyme.
3.
3. Since the single-ion-dependent adenosinetriphosphatase activity was revealed merely by a physical change in the method of preparation (sonication), it is reasonable to suspect that it and the Na+-plus-K+-dependent activity are different manifestations of a single enzymic activity.
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