Possible involvement of adenylylation in the modification of a 26 kDa protein in rat parotid acinar cells

International Journal of Biochemistry Pub Date : 1994-09-01 DOI:10.1016/0020-711X(94)90132-5

Miki Hara-Yokoyama, Hiroshi Sugiya, Shunsuke Furuyama

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引用次数: 1

Abstract

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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腺苷化可能参与大鼠腮腺腺泡细胞中26 kDa蛋白的修饰

1.1. 2.2.在大鼠腮腺腺泡细胞中，研究了一种翻译后修饰蛋白的腺苷化。当细胞与[2,8- 3h]ATP孵育时，几种蛋白质，包括颗粒部分中的26 kDa蛋白，被标记。在cAMP和3-异丁基甲基黄嘌呤存在下，用[α-32P]ATP孵育细胞，观察到26kda蛋白的32p标记。经蛇毒磷酸二酯酶处理后，[32P]AMP从26kDa蛋白中释放出来。当细胞用[γ-32P]ATP.5.5标记时，没有观察到这种释放。含有[α-32P]ATP的蛋白的32p标记模式与含有[腺苷- 32p]NAD+.6.6的蛋白明显不同。结果表明，26 kDa蛋白是大鼠腮腺腺泡细胞腺苷化底物之一。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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International Journal of Biochemistry

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