Developmental regulation of proteolytic activities and subunit pattern of 20 S proteasome in chick embryonic muscle

The proteolytic activities of the 20 S proteasome were found to change in their levels during the development of chick embryonic muscle. The peptide-cleaving activities against N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and N-benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy- beta -naphthylamide grad...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-01, Vol.266 (24), p.15646-15649
Main Authors: Ahn, Joon Young, Hong, Seung Oh, Kwak, Kyu Bong, Kang, Shin Sung, Tanaka, Keiji, Ichihara, Akira, Ha, Doo Bong, Chung, Chin Ha
Format: Article
Language:English
Subjects:
activity
chickens
development
muscles
proteasomes
proteinase
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Summary:The proteolytic activities of the 20 S proteasome were found to change in their levels during the development of chick embryonic muscle. The peptide-cleaving activities against N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin and N-benzyloxycarbonyl-Ala-Arg-Arg-4-methoxy- beta -naphthylamide gradually decreased with the time of development. On the other hand, the casein-degrading activity in the presence of poly-L-lysine markedly increased from embryonic day 11 and reached a maximal level by day 17. These changes appeared to be tissue-specific because little or no change in any of the proteolytic activities was observed with developing embryonic brain, while dramatic alterations occurred in the extents of the peptide hydrolyses in liver.
ISSN:0021-9258