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胰腺酶原颗粒细胞质表面暴露蛋白的鉴定

Identification of the proteins exposed on the cytoplasmic surface of the pancreatic zymogen granule.

作者信息

LeBel D, Beattie M

出版信息

Biochim Biophys Acta. 1984 Feb 15;769(3):622-4. doi: 10.1016/0005-2736(84)90061-0.

Abstract

Lactoperoxidase-catalyzed 125I-iodination was used to label pancreatic zymogen granules. Membrane proteins facing the cytoplasmic surface were specifically labeled. Two low molecular weight proteins of 17 000 and 15 000 were intensely labeled at 0 degree C. Another small 13 kDa protein was strongly iodinated at 25 degrees C along with some others, including the 29 kDa subunit of the ATP diphosphohydrolase. The major glycoprotein of the granule membrane was not iodinated but the presence of an iodinated 80 kDa protein suggests that proteolytic fragments of the 92 kDa glycoprotein were accessible to iodination on the intact granule. These proteins localized on the cytoplasmic surface of the granule are believed to play a major role in the exocytotic phenomenon of the exocrine pancreas.

摘要

乳过氧化物酶催化的¹²⁵I碘化法被用于标记胰腺酶原颗粒。面向细胞质表面的膜蛋白被特异性标记。在0℃时,两种分子量分别为17000和15000的低分子量蛋白被强烈标记。另一种13 kDa的小蛋白在25℃时与其他一些蛋白一起被强烈碘化,包括ATP二磷酸水解酶的29 kDa亚基。颗粒膜的主要糖蛋白未被碘化,但一种碘化的80 kDa蛋白的存在表明,完整颗粒上92 kDa糖蛋白的蛋白水解片段可被碘化。这些定位于颗粒细胞质表面的蛋白被认为在外分泌胰腺的胞吐现象中起主要作用。

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