Post-translational Modification of K>Casein in the Golgi Apparatus of Mid-lactating MammaryGlands from Rat and Cow
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概要
- 論文の詳細を見る
Bovine κ-casein, a phosphoglycoprotein, has mucin-type carbohydrate chains. Subcellular distribution of enzymes that take part in the post-translational modification of κ-casein was examined. In lactating mammaryglands from rats and cows, .N-acetyl-galactosaminyl transferase, galactosyl transferase, sialyl transferase, and casein kinase were localized specifically in the Golgi apparatus. The substrate specificities indicate that these enzymes are actually responsible for the processing of κ-casein. The presence of a phosphate group attached to K>casein did not affect the rate of glycosylation by N-acetyl-galactosaminyl transferase, while the presence of carbohydrate chains attached to κ-casein strongly reduced the rate of phosphorylation by casein kinase. These results suggest that in the Golgi apparatus, phosphorylation of K-casein precedes glycosylation.
- 社団法人 日本農芸化学会の論文
著者
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CHIBA Hideo
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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Tsuda Eisuke
Department Of Food Science And Technology Faculty Of Agriculture Kyoto University
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Sasaki Ryuzo
Department Of Food Science And Technology Faculty Of Agriculture Kyoto University
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Yoshikawa Masaaki
Department Of Clinical Pharmacology School Of Medicine Tokai University
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Takeuchi Makoto
Department Of Biology Faculty Of Science Okayama University
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