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. 1972 Oct;112(1):585–592. doi: 10.1128/jb.112.1.585-592.1972

Specific Removal of Proteins from the Envelope of Escherichia coli by Protease Treatments

Masayori Inouye 1, Mei-Lan Yee 1
PMCID: PMC251448  PMID: 4116755

Abstract

When the envelope fraction of Escherichia coli was treated by trypsin, about 40% of total envelope proteins were removed from the fraction without changing its phospholipid content. Analysis of envelope proteins by acrylamide gel electrophoresis in 0.5% sodium dodecyl sulfate revealed that trypsin treatment was very specific; one of the major proteins (molecular weight, 38,000) and all proteins of molecular weight greater than 70,000 were completely removed by the treatment. On the other hand, three other major proteins were found to be resistant to the treatment, including protein Y, which was previously shown to be related to deoxyribonucleic acid replication. The trypsin treatment of the envelope fractions composed of a five electron-dense layered structure formed vesicles with a triple-layered membrane (two electron-dense layers). Pronase treatment of the envelope fraction removed about 60% of the envelope proteins without changing its phospholipid content. A major protein of molecular weight of 58,000 was found to be the only protein resistant to the Pronase treatment. Application of these treatments is useful for purification and structural studies of envelope proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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