Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits

scientific article published on July 15, 1983

Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/0003-9861(83)90242-4
P953full work available at URLhttps://api.elsevier.com/content/article/PII:0003986183902424?httpAccept=text/xml
https://api.elsevier.com/content/article/PII:0003986183902424?httpAccept=text/plain
P698PubMed publication ID6347072

P2093author name stringC. H. Chung
A. L. Goldberg
K. H. Swamy
P2860cites workProtein measurement with the Folin phenol reagentQ20900776
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The mechanism of protein secretion across membranesQ59081348
E. coli contains eight soluble proteolytic activities, one being ATP dependentQ59098559
ATP-stimulated endoprotease is associated with the cell membrane of E. coliQ67293053
Variable subunit structure of lysine-sensitive aspartylkinase from Escherichia coli TIR-8Q69254807
Deficiency in Initiation Factors of Protein Synthesis in Stationary-Phase Escherichia coliQ69377979
Identification of protease IV of E, coliQ70158564
A STUDY OF THE UREA-PRODUCED SUBUNITS OF BETA-GALACTOSIDASEQ76562428
A spectrophotometric determination of trypsin and chymotrypsinQ78720498
Cleavage of the haem-protein link by acid methylethylketoneQ79285559
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P433issue2
P407language of work or nameEnglishQ1860
P921main subjectbiochemistryQ7094
biophysicsQ7100
Escherichia coliQ25419
serine endopeptidaseQ420032
periplasmic proteinsQ76829424
P304page(s)543-554
P577publication date1983-07-01
1983-07-15
P1433published inArchives of Biochemistry and BiophysicsQ635818
P1476titleIsolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits
Isolation and characterization of protease Do from Escherichia coli, a large serine protease containing multiple subunits
P478volume224