Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila

Olga G. Zatsepina; Alexander A. Karavanov; David G. Garbuz; Victoria Shilova; Peter Tornatore; Michael B. Evgen'ev

doi:10.1379/CSC-71.1

Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila

Olga G. Zatsepina, Alexander A. Karavanov, David G. Garbuz, Victoria Shilova, Peter Tornatore, Michael B. Evgen'ev

Research output: Contribution to journal › Article › peer-review

Abstract

The 70-kDa heat shock protein (Hsp) family in all Drosophila species includes 2 environmentally inducible family members, Hsp70 and Hsp68. Two-dimensional gel electrophoresis revealed an unusual pattern of heat shock-inducible proteins in the species of the virilis group. Trypsin fingerprinting and microsequencing of tryptic peptides using ProteinChip Array technology identified the major isoelectric variants of Hsp70 family, including Hsp68 isoforms that differ in both molecular mass and isoelectric point from those in Drosophila melanogaster. The peculiar electrophoretic mobility is consistent with the deduced amino acid sequence of corresponding hsp genes from the species of the virilis group.

Original language	English
Pages (from-to)	12-16
Number of pages	5
Journal	Cell Stress and Chaperones
Volume	10
Issue number	1
DOIs	https://doi.org/10.1379/CSC-71.1
State	Published - Mar 2005
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Cell Biology

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title = "Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila",

abstract = "The 70-kDa heat shock protein (Hsp) family in all Drosophila species includes 2 environmentally inducible family members, Hsp70 and Hsp68. Two-dimensional gel electrophoresis revealed an unusual pattern of heat shock-inducible proteins in the species of the virilis group. Trypsin fingerprinting and microsequencing of tryptic peptides using ProteinChip Array technology identified the major isoelectric variants of Hsp70 family, including Hsp68 isoforms that differ in both molecular mass and isoelectric point from those in Drosophila melanogaster. The peculiar electrophoretic mobility is consistent with the deduced amino acid sequence of corresponding hsp genes from the species of the virilis group.",

author = "Zatsepina, {Olga G.} and Karavanov, {Alexander A.} and Garbuz, {David G.} and Victoria Shilova and Peter Tornatore and Evgen'ev, {Michael B.}",

year = "2005",

month = mar,

doi = "10.1379/CSC-71.1",

language = "English",

volume = "10",

pages = "12--16",

journal = "Cell Stress and Chaperones",

issn = "1355-8145",

publisher = "Elsevier",

number = "1",

}

Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila. / Zatsepina, Olga G.; Karavanov, Alexander A.; Garbuz, David G. et al.
In: Cell Stress and Chaperones, Vol. 10, No. 1, 03.2005, p. 12-16.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila

AU - Zatsepina, Olga G.

AU - Karavanov, Alexander A.

AU - Garbuz, David G.

AU - Shilova, Victoria

AU - Tornatore, Peter

AU - Evgen'ev, Michael B.

PY - 2005/3

Y1 - 2005/3

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AB - The 70-kDa heat shock protein (Hsp) family in all Drosophila species includes 2 environmentally inducible family members, Hsp70 and Hsp68. Two-dimensional gel electrophoresis revealed an unusual pattern of heat shock-inducible proteins in the species of the virilis group. Trypsin fingerprinting and microsequencing of tryptic peptides using ProteinChip Array technology identified the major isoelectric variants of Hsp70 family, including Hsp68 isoforms that differ in both molecular mass and isoelectric point from those in Drosophila melanogaster. The peculiar electrophoretic mobility is consistent with the deduced amino acid sequence of corresponding hsp genes from the species of the virilis group.

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Use of surface-enhanced laser desorption ionization-time-of-flight to identify heat shock protein 70 isoforms in closely related species of the virilis group of Drosophila

Abstract

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