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由鼠淋巴细胞系S-49.1 TB-2-3表达的Thy-1.2同种异体抗原的蛋白质性质。

The protein nature of the Thy-1.2 alloantigen as expressed by the murin lymphoblastoid line S-49.1 TB-2-3.

作者信息

Kucich U N, Bennett J C, Johnson B J

出版信息

J Immunol. 1975 Sep;115(3):626-30.

PMID:1151070
Abstract

This preliminary study was undertaken to investigate the chemical nature of the Thy-1.2 antigen expressed on the murine cell line S-49.1 TB-2-3 (S-49). The presence of the Thy-1.2 antigen was indicated by the inhibition of AKR anti-C3-Thy-1.2 serum induced lysis of 51Cr-primed target cells. It was found that limited digestion of S-49 cells with crude papain yielded a Thy-1.2-containing solution. The protein nature of the Thy-1.2 antigen obtained in this manner was indicated by changes after proteolytic digestion. Separate digestions with crystalline papain, insolubilized papain, and insolubilized protease all destroyed the Thy-1.2 activity. These results suggest that the protein moiety is necessary for Thy-1.2 activity.

摘要

本初步研究旨在调查鼠细胞系S-49.1 TB-2-3(S-49)上表达的Thy-1.2抗原的化学性质。AKR抗C3-Thy-1.2血清诱导的对51Cr预标记靶细胞的裂解受到抑制,表明存在Thy-1.2抗原。发现用粗木瓜蛋白酶对S-49细胞进行有限消化可得到含Thy-1.2的溶液。通过蛋白水解消化后的变化表明以这种方式获得的Thy-1.2抗原具有蛋白质性质。用结晶木瓜蛋白酶、不溶性木瓜蛋白酶和不溶性蛋白酶分别进行消化均破坏了Thy-1.2活性。这些结果表明蛋白质部分对于Thy-1.2活性是必需的。

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