A NOVEL ACID PROTEINASE RELEASED BY HYBRIDOMA CELLS

被引：19

作者：

KARL, DW ^{[1
]}

DONOVAN, M ^{[1
]}

FLICKINGER, MC ^{[1
]}

机构：

[1] UNIV MINNESOTA,DEPT BIOCHEM,ST PAUL,MN 55108

来源：

CYTOTECHNOLOGY | 1990年 / 3卷 / 02期

关键词：

acid proteinase; cell culture; hybridoma; immunoglobulin cleavage; lysosomal proteinases; recycling reactor;

D O I：

10.1007/BF00143678

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

An acid proteinase has been detected in culture supernate of the 9.2.27 murine hybridoma. This enzyme extensively degrades albumin and transferrin during short incubations at pH 3 and below. Limited proteolysis of the 9.2.27 IgG2a appears to occur in the culture supernate. Proteolysis is enhanced at low pH in the presence of urea or 1 M acetic acid. The proteinase activity accumulates in continuous perfusion, total cell recycle cultures, beginning during exponential growth of the hybridoma. It is destroyed by boiling and blocked by pepstatin, but not by inhibitors of cysteine or serine proteinases or by EDTA. The low pH optimum may distinguish this enzyme from the known rat and mouse aspartic acid proteinases including cathepsin D and cathepsin E. © 1990 Kluwer Academic Publishers.

引用

页码：157 / 169

页数：13

共 23 条

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