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来自人红细胞胞质部分的核糖核酸酶。

Ribonuclease from cytosolic fraction of human erythrocytes.

作者信息

Czajkowska B, Naskalski J W, Sznajd J

出版信息

Clin Chim Acta. 1986 Jan 15;154(1):19-27. doi: 10.1016/0009-8981(86)90084-7.

DOI:10.1016/0009-8981(86)90084-7
PMID:3943222
Abstract

Ribonuclease (RNase) activity is detectable in only one third of specimens of human erythrocyte haemolysates. On the other hand, treatment of erythrocytic cytosoles with sulphosalicylic acid reveals an inhibitor-bound RNase activity which is present in all erythrocyte specimens studied. The level of the erythrocyte inhibitor-bound RNase activity is comparable to that in human lymphocytes. Isolated RNase from the cytosolic fraction of human erythrocytes is poly-C avid RNase with maximum activity at pH 6.5. The enzyme is resistant to treatment with strong acids and heating up to 95 degrees C. Molecular filtration of the erythrocyte RNase shows that it is composed of two fractions differing in molecular mass, 19 000 and 15 000. No difference in enzymic properties between these fractions was found. The general properties of erythrocyte cytosolic RNase are much like those of acid RNases of human granulocytes and lymphocytes. As the erythrocytes do not metabolize RNA no function for the inhibitor-bound RNase can be suggested. Assuming that the observed erythrocyte RNase is the residual enzyme, persisting in the cell since it was functioning in the nucleated erythrocyte precursors, one may surmise that levels of free and inhibitor-bound erythrocyte RNase activity may be related to the normality or abnormality of erythrocyte maturation.

摘要

核糖核酸酶(RNase)活性仅在三分之一的人红细胞溶血产物样本中可检测到。另一方面,用磺基水杨酸处理红细胞胞质溶胶后发现一种与抑制剂结合的RNase活性,在所研究的所有红细胞样本中均存在。红细胞中与抑制剂结合的RNase活性水平与人类淋巴细胞中的相当。从人红细胞胞质部分分离出的RNase是一种多聚C亲和性RNase,在pH 6.5时活性最高。该酶对强酸处理和加热至95摄氏度具有抗性。红细胞RNase的分子过滤显示它由分子量不同的两个部分组成,分别为19000和15000。未发现这些部分在酶学性质上有差异。红细胞胞质RNase的一般性质与人类粒细胞和淋巴细胞的酸性RNase非常相似。由于红细胞不代谢RNA,因此无法推测与抑制剂结合的RNase的功能。假设观察到的红细胞RNase是残留酶,自其在有核红细胞前体中发挥作用以来一直存在于细胞中,那么可以推测游离和与抑制剂结合的红细胞RNase活性水平可能与红细胞成熟的正常或异常有关。

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