EVIDENCE FOR PHOSPHORYL MOIETIES IN A PROTEINASE FROM DICTYOSTELIUM-DISCOIDEIUM

被引：8

作者：

GUSTAFSON, GL

THON, LA

机构：

[1] Department of Microbiology University of Montana, Missoula

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 86卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91765-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A proteinase (called proteinase I) present in myxamoebae of the cellular slime mold, D. discoideum, was labeled in vivo with [32P] by growth of cells on media containing [32P] Pi. The labeled proteinase was purified to apparent homogeneity and characterized by dissociation chromatography and quantitative immune-precipitin analysis. The phosphoryl moieties were tightly associated [presumably covalently bonded] with the polypeptide subunits of proteinase I.

引用

页码：667 / 673

页数：7

共 10 条

[1]

Ames B.N., 1966, METHOD ENZYMOL, V8, P115, DOI [DOI 10.1016/0076-6879(66)08014-5, 10.1016/0076-6879(66)08014-5]

[2]

FISH WW, 1969, J BIOL CHEM, V244, P4989

[3] UDP-GLUCOSE PYROPHOSPHORYLASE SYNTHESIS IN MYXAMOEBAE OF DICTYOSTELIUM-DISCOIDEUM [J].