{"title":"腺苷化可能参与大鼠腮腺腺泡细胞中26 kDa蛋白的修饰","authors":"Miki Hara-Yokoyama, Hiroshi Sugiya, Shunsuke Furuyama","doi":"10.1016/0020-711X(94)90132-5","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Adenylylation, a posttranslational modification of proteins, was investigated in saponin-permeabilized acinar cells of the rat parotid gland.</p></span></li><li><span>2.</span><span><p>2. When cells were incubated with [2,8-<sup>3</sup>H]ATP, several proteins, including a 26 kDa protein in the particulate fraction, were labeled.</p></span></li><li><span>3.</span><span><p>3. Upon incubation of cells with [α-<sup>32</sup>P]ATP in the presence of cAMP and 3-isobutyl-lmethylxanthine, <sup>32</sup>P-labeling of the 26 kDa protein was observed.</p></span></li><li><span>4.</span><span><p>4. After treatment with snake venom phosphodiesterase, [<sup>32</sup>P]AMP was released from the 26kDa protein. Such release was not observed when cells were labeled with [γ-<sup>32</sup>P]ATP.</p></span></li><li><span>5.</span><span><p>5. The <sup>32</sup>P-labeling pattern of proteins with [α-<sup>32</sup>P]ATP was clearly different from that with [<em>adenylate</em>-<sup>32</sup>P]NAD<sup>+</sup>.</p></span></li><li><span>6.</span><span><p>6. The results suggest that the 26 kDa protein is one of the adenylylation substrates in rat parotid acinar cells.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1103-1109"},"PeriodicalIF":0.0000,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90132-5","citationCount":"1","resultStr":"{\"title\":\"Possible involvement of adenylylation in the modification of a 26 kDa protein in rat parotid acinar cells\",\"authors\":\"Miki Hara-Yokoyama, Hiroshi Sugiya, Shunsuke Furuyama\",\"doi\":\"10.1016/0020-711X(94)90132-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Adenylylation, a posttranslational modification of proteins, was investigated in saponin-permeabilized acinar cells of the rat parotid gland.</p></span></li><li><span>2.</span><span><p>2. When cells were incubated with [2,8-<sup>3</sup>H]ATP, several proteins, including a 26 kDa protein in the particulate fraction, were labeled.</p></span></li><li><span>3.</span><span><p>3. Upon incubation of cells with [α-<sup>32</sup>P]ATP in the presence of cAMP and 3-isobutyl-lmethylxanthine, <sup>32</sup>P-labeling of the 26 kDa protein was observed.</p></span></li><li><span>4.</span><span><p>4. After treatment with snake venom phosphodiesterase, [<sup>32</sup>P]AMP was released from the 26kDa protein. Such release was not observed when cells were labeled with [γ-<sup>32</sup>P]ATP.</p></span></li><li><span>5.</span><span><p>5. The <sup>32</sup>P-labeling pattern of proteins with [α-<sup>32</sup>P]ATP was clearly different from that with [<em>adenylate</em>-<sup>32</sup>P]NAD<sup>+</sup>.</p></span></li><li><span>6.</span><span><p>6. The results suggest that the 26 kDa protein is one of the adenylylation substrates in rat parotid acinar cells.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 9\",\"pages\":\"Pages 1103-1109\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90132-5\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94901325\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94901325","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Possible involvement of adenylylation in the modification of a 26 kDa protein in rat parotid acinar cells
1.
1. Adenylylation, a posttranslational modification of proteins, was investigated in saponin-permeabilized acinar cells of the rat parotid gland.
2.
2. When cells were incubated with [2,8-3H]ATP, several proteins, including a 26 kDa protein in the particulate fraction, were labeled.
3.
3. Upon incubation of cells with [α-32P]ATP in the presence of cAMP and 3-isobutyl-lmethylxanthine, 32P-labeling of the 26 kDa protein was observed.
4.
4. After treatment with snake venom phosphodiesterase, [32P]AMP was released from the 26kDa protein. Such release was not observed when cells were labeled with [γ-32P]ATP.
5.
5. The 32P-labeling pattern of proteins with [α-32P]ATP was clearly different from that with [adenylate-32P]NAD+.
6.
6. The results suggest that the 26 kDa protein is one of the adenylylation substrates in rat parotid acinar cells.
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