DNase-I-like enzyme from the carp liver—Inhibition by muscle and endogenous actin

International Journal of Biochemistry Pub Date : 1994-09-01 DOI:10.1016/0020-711X(94)90137-6

Maria Malicka-Blaszkiewicz, Ilona Majcher, Dorota Nowak

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引用次数: 5

Abstract

1.
1. DNase-I-like activity occurs in the carp (Cyprinus carpio) liver cytosol (supernatant 105,000g).
2.
2. The enzyme resembles DNase I from bovine pancreas in respect to the molecular mass (~31 kDa), pH (7.4) and ion requirements (Mg²⁺, Ca²⁺) and the ability to degrade native as well as denatured DNA.
3.
3. As judged by comparison of DNase zymograms obtained after native- and SDS-PAGE, the enzyme occurs in the three molecular forms of similar molecular weight and different charges.
4.
4. All these forms are inhibited by rabbit skeletal muscle actin as well as by endogenous actin isolated from the carp liver cytosol.
5.
5. DNase from the carp liver cytosol does not interact with the antibodies directed against DNase I from bovine pancreas and against DNase I from the rat and bovine parotid glands.

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来自鲤鱼肝脏的dna - i样酶——肌肉和内源性肌动蛋白的抑制作用

1.1. 2.2.鲤(Cyprinus carpio)肝细胞质(上清105,000g)中存在dna - i样活性。在分子质量(~31 kDa)、pH值(7.4)和离子需求(Mg2+、Ca2+)以及降解天然和变性dna的能力方面，该酶与牛胰腺中的DNase I相似。通过比较native-和SDS-PAGE得到的DNase酶谱判断，该酶以三种分子量相近、电荷不同的分子形式存在。兔骨骼肌肌动蛋白和从鲤鱼肝细胞质中分离的内源性肌动蛋白均能抑制上述几种形式。来自鲤鱼肝细胞质的dna酶与来自牛胰腺的dna酶I抗体以及来自大鼠和牛腮腺的dna酶I抗体不相互作用。

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International Journal of Biochemistry

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