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发育中大鼠肝脏的溶酶体水解酶活性

Lysosomal hydrolase activities in the developing rat liver.

作者信息

Messina M, Tessitore L, Musi M, Baccino F M, Fiszer-Szafarz B, Nadal C

出版信息

Boll Soc Ital Biol Sper. 1980 Jan 15;56(1):27-32.

PMID:6776967
Abstract

The specific activity of three lysosomal proteinases (cathepsins B1, D, and L) as well as acid phosphatase and beta-galactosidase has been determined in the liver of both 7-10 day-old and young adult rats. Cathepsin B1 in suckling rats is markedly lower than in adults, while cathepsin D is only moderately lower and cathepsin L does not significantly differ. The activity of acid phosphatase is similar in the two groups of animals whereas that of beta-galactosidase in suckling rats is approx. twice as high as in adults. The activity of lysosomal hydrolases thus appears to be regulated individually during the development. Moreover it is suggested that the low activity of cathepsin B1 may be related to the low rate of cell protein catabolism characteristic of the developing liver (Conde and Scornik, 1977).

摘要

已测定7至10日龄幼鼠和成年大鼠肝脏中三种溶酶体蛋白酶(组织蛋白酶B1、D和L)以及酸性磷酸酶和β-半乳糖苷酶的比活性。乳鼠中的组织蛋白酶B1明显低于成年鼠,而组织蛋白酶D仅略低,组织蛋白酶L则无显著差异。两组动物的酸性磷酸酶活性相似,而乳鼠中的β-半乳糖苷酶活性约为成年鼠的两倍。因此,溶酶体水解酶的活性在发育过程中似乎是单独调节的。此外,有人认为组织蛋白酶B1的低活性可能与发育中肝脏细胞蛋白质分解代谢率低有关(康德和斯科尔尼克,1977年)。

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