Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria

Carsten Nøhr; Peter Højrup; Svend Olav Andersen

doi:10.1016/0965-1748(92)90095-V

Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria

Carsten Nøhr, Peter Højrup, Svend Olav Andersen^*

^*Corresponding author for this work

Department of Biochemistry and Molecular Biology

University of Copenhagen

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The cuticle from mid-instar fifth stage locust (Locusta migratoria) contains close to a hundred extractable proteins, which can be separated by means of two-dimensional polyacrylamide gel-electrophoresis. A few of the proteins have been purified by ion-exchange chromatography, and the complete amino acid sequence has been determined for two of them. They are probably of endocuticular origin. Both proteins are small (33 and 88 amino acid residues, respectively), and none of them are secondarily modified. The sequence of the smallest protein shows pronounced similarity to local sequences found in proteins from pharate adult cuticle of the same species, whereas the other protein shows no similarities to cuticular proteins obtained from this or from other insect species.

Original language	English
Journal	Insect Biochemistry and Molecular Biology
Volume	22
Issue number	1
Pages (from-to)	19-24
ISSN	0965-1748
DOIs	https://doi.org/10.1016/0965-1748(92)90095-V
Publication status	Published - Jan 1992

Keywords

cuticle proteins
primary structure
protein purification
structural proteins
two-dimensional electrophoresis

Documents & Links

10.1016/0965-1748(92)90095-V

Cite this

@article{1b68038342f6449595b4a835040d34f2,

title = "Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria",

abstract = "The cuticle from mid-instar fifth stage locust (Locusta migratoria) contains close to a hundred extractable proteins, which can be separated by means of two-dimensional polyacrylamide gel-electrophoresis. A few of the proteins have been purified by ion-exchange chromatography, and the complete amino acid sequence has been determined for two of them. They are probably of endocuticular origin. Both proteins are small (33 and 88 amino acid residues, respectively), and none of them are secondarily modified. The sequence of the smallest protein shows pronounced similarity to local sequences found in proteins from pharate adult cuticle of the same species, whereas the other protein shows no similarities to cuticular proteins obtained from this or from other insect species.",

keywords = "cuticle proteins, primary structure, protein purification, structural proteins, two-dimensional electrophoresis",

author = "Carsten N{\o}hr and Peter H{\o}jrup and {Olav Andersen}, Svend",

year = "1992",

month = jan,

doi = "10.1016/0965-1748(92)90095-V",

language = "English",

volume = "22",

pages = "19--24",

journal = "Insect Biochemistry and Molecular Biology",

issn = "0965-1748",

publisher = "Elsevier",

number = "1",

}

Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria. / Nøhr, Carsten; Højrup, Peter; Olav Andersen, Svend.
In: Insect Biochemistry and Molecular Biology, Vol. 22, No. 1, 01.1992, p. 19-24.

Research output: Contribution to journal › Journal article › Research › peer-review

TY - JOUR

T1 - Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria

AU - Nøhr, Carsten

AU - Højrup, Peter

AU - Olav Andersen, Svend

PY - 1992/1

Y1 - 1992/1

N2 - The cuticle from mid-instar fifth stage locust (Locusta migratoria) contains close to a hundred extractable proteins, which can be separated by means of two-dimensional polyacrylamide gel-electrophoresis. A few of the proteins have been purified by ion-exchange chromatography, and the complete amino acid sequence has been determined for two of them. They are probably of endocuticular origin. Both proteins are small (33 and 88 amino acid residues, respectively), and none of them are secondarily modified. The sequence of the smallest protein shows pronounced similarity to local sequences found in proteins from pharate adult cuticle of the same species, whereas the other protein shows no similarities to cuticular proteins obtained from this or from other insect species.

AB - The cuticle from mid-instar fifth stage locust (Locusta migratoria) contains close to a hundred extractable proteins, which can be separated by means of two-dimensional polyacrylamide gel-electrophoresis. A few of the proteins have been purified by ion-exchange chromatography, and the complete amino acid sequence has been determined for two of them. They are probably of endocuticular origin. Both proteins are small (33 and 88 amino acid residues, respectively), and none of them are secondarily modified. The sequence of the smallest protein shows pronounced similarity to local sequences found in proteins from pharate adult cuticle of the same species, whereas the other protein shows no similarities to cuticular proteins obtained from this or from other insect species.

KW - cuticle proteins

KW - primary structure

KW - protein purification

KW - structural proteins

KW - two-dimensional electrophoresis

U2 - 10.1016/0965-1748(92)90095-V

DO - 10.1016/0965-1748(92)90095-V

M3 - Journal article

AN - SCOPUS:38249015289

SN - 0965-1748

VL - 22

SP - 19

EP - 24

JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

IS - 1

ER -

Primary structure of two low molecular weight proteins isolated from cuticle of fifth instar nymphs of the migratory locust, Locusta migratoria

Abstract

Keywords

Documents & Links

Fingerprint

Cite this