Expression of jumper ant (Myrmecia pilosula) venom allergens: Post-translational processing of allergen gene products

G. R. Donovan; M. D. Street; T. Tetaz; A. I. Smith; D. Alewood; P. Alewood; S. K. Sutherland; B. A. Baldo

Expression of jumper ant (Myrmecia pilosula) venom allergens: Post-translational processing of allergen gene products

G. R. Donovan
, M. D. Street
, T. Tetaz
, A. I. Smith
, D. Alewood
, P. Alewood
, S. K. Sutherland
, B. A. Baldo

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

Abstract

N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.

Original language	English
Pages (from-to)	877-885
Number of pages	9
Journal	Biochemistry and Molecular Biology International
Volume	39
Issue number	5
Publication status	Published - 14 Sept 1996
Externally published	Yes

Keywords

Allergens
Electrophoresis
Gene expression
Post-translational processing
Venom

Cite this

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title = "Expression of jumper ant (Myrmecia pilosula) venom allergens: Post-translational processing of allergen gene products",

abstract = "N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.",

keywords = "Allergens, Electrophoresis, Gene expression, Post-translational processing, Venom",

author = "Donovan, \{G. R.\} and Street, \{M. D.\} and T. Tetaz and Smith, \{A. I.\} and D. Alewood and P. Alewood and Sutherland, \{S. K.\} and Baldo, \{B. A.\}",

year = "1996",

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journal = "Biochemistry and Molecular Biology International",

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T1 - Expression of jumper ant (Myrmecia pilosula) venom allergens

T2 - Post-translational processing of allergen gene products

AU - Donovan, G. R.

AU - Street, M. D.

AU - Tetaz, T.

AU - Smith, A. I.

AU - Alewood, D.

AU - Alewood, P.

AU - Sutherland, S. K.

AU - Baldo, B. A.

PY - 1996/9/14

Y1 - 1996/9/14

N2 - N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.

AB - N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.

KW - Allergens

KW - Electrophoresis

KW - Gene expression

KW - Post-translational processing

KW - Venom

UR - https://www.scopus.com/pages/publications/0029760226

M3 - Article

C2 - 8866004

AN - SCOPUS:0029760226

SN - 1039-9712

VL - 39

SP - 877

EP - 885

JO - Biochemistry and Molecular Biology International

JF - Biochemistry and Molecular Biology International

IS - 5

ER -

Expression of jumper ant (Myrmecia pilosula) venom allergens: Post-translational processing of allergen gene products

Abstract

Keywords

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