Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

Research output: Contribution to journalArticlepeer-review

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Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin. / Morgan, P J; Harrison, G; Freestone, P P; Crane, D; Rowe, A J; Mitchell, T J; Andrew, P W; Gilbert, R J.

In: FEBS Letters, Vol. 412, No. 3, 04.08.1997, p. 563-7.

Research output: Contribution to journalArticlepeer-review

Harvard

Morgan, PJ, Harrison, G, Freestone, PP, Crane, D, Rowe, AJ, Mitchell, TJ, Andrew, PW & Gilbert, RJ 1997, 'Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin', FEBS Letters, vol. 412, no. 3, pp. 563-7.

APA

Morgan, P. J., Harrison, G., Freestone, P. P., Crane, D., Rowe, A. J., Mitchell, T. J., Andrew, P. W., & Gilbert, R. J. (1997). Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin. FEBS Letters, 412(3), 563-7.

Vancouver

Author

Morgan, P J ; Harrison, G ; Freestone, P P ; Crane, D ; Rowe, A J ; Mitchell, T J ; Andrew, P W ; Gilbert, R J. / Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin. In: FEBS Letters. 1997 ; Vol. 412, No. 3. pp. 563-7.

Bibtex

@article{72a5b371360a4bf38e09ef62a126c897,
title = "Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin",
abstract = "Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.",
keywords = "Bacterial Proteins, Circular Dichroism, Endopeptidase K, Hemolysis, Hydrolysis, Liposomes, Peptide Fragments, Protein Binding, Spectrometry, Fluorescence, Streptolysins, Structure-Activity Relationship",
author = "Morgan, {P J} and G Harrison and Freestone, {P P} and D Crane and Rowe, {A J} and Mitchell, {T J} and Andrew, {P W} and Gilbert, {R J}",
year = "1997",
month = aug,
day = "4",
language = "English",
volume = "412",
pages = "563--7",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

AU - Morgan, P J

AU - Harrison, G

AU - Freestone, P P

AU - Crane, D

AU - Rowe, A J

AU - Mitchell, T J

AU - Andrew, P W

AU - Gilbert, R J

PY - 1997/8/4

Y1 - 1997/8/4

N2 - Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.

AB - Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.

KW - Bacterial Proteins

KW - Circular Dichroism

KW - Endopeptidase K

KW - Hemolysis

KW - Hydrolysis

KW - Liposomes

KW - Peptide Fragments

KW - Protein Binding

KW - Spectrometry, Fluorescence

KW - Streptolysins

KW - Structure-Activity Relationship

M3 - Article

C2 - 9276467

VL - 412

SP - 563

EP - 567

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -