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PMID: 2900235 Published · ppublish English Journal Article

Purification of the Escherichia coli type 1 pilin and minor pilus proteins and partial characterization of the adhesin protein.

Journal of bacteriology ·Vol. 170 ·No. 8 ·1988-08-00 ·Pages 3350-8

Hanson MS, Hempel J, Brinton CC

Abstract

Type 1 pili of Escherichia coli contain three integral minor proteins with apparent molecular weights (Mr) of 28,000 (28K protein), 16,500, and 14,500 attached to rods composed of Mr-17,000 pilin subunits (Hanson and Brinton, Nature [London] 322:265-268). We describe here an improvement on our earlier method of pilus purification, which gives higher yields and higher purity. Also reported are methods allowing fractionation of intact type 1 pili into rods of pure pilin and free minor proteins, as well as fractionation of the 28K tip adhesion protein from the 16.5K and 14.5K proteins. We have determined the amino acid composition and amino-terminal sequence of the adhesion protein. This sequence shows limited homology with the amino-terminal sequences of several E. coli pilins, including type 1.

MeSH Terms
Adhesins, Escherichia coli Amino Acid Sequence Bacterial Adhesion Bacterial Outer Membrane Proteins/analysis,isolation & purification Electrophoresis, Polyacrylamide Gel Escherichia coli/analysis,ultrastructure Fimbriae Proteins Fimbriae, Bacterial/analysis Molecular Sequence Data Sequence Homology, Nucleic Acid
Chemicals
Adhesins, Escherichia coli Bacterial Outer Membrane Proteins Fimbriae Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hanson M S
Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.
Hempel J
Brinton C C
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1988-08-00
Pages
3350-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC211301
Subset
IM
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