PRIMARY STRUCTURE OF 2 LOW-MOLECULAR-WEIGHT PROTEINS ISOLATED FROM CUTICLE OF 5TH INSTAR NYMPHS OF THE MIGRATORY LOCUST, LOCUSTA-MIGRATORIA

被引：18

作者：

NOHR, C

HOJRUP, P

ANDERSEN, SO

机构：

[1] AUGUST KROGH INST,INST BIOL CHEM A,UNIV SPARKEN 13,DK-2100 COPENHAGEN,DENMARK

[2] ODENSE UNIV,DEPT MOLEC BIOL,DK-5230 ODENSE,DENMARK

来源：

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1992年 / 22卷 / 01期

关键词：

CUTICLE PROTEINS; PRIMARY STRUCTURE; PROTEIN PURIFICATION; STRUCTURAL PROTEINS; 2-DIMENSIONAL ELECTROPHORESIS;

D O I：

10.1016/0965-1748(92)90095-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：19 / 24

页数：6

共 32 条

[21] STRUCTURE AND EXPRESSION OF A MANDUCA-SEXTA LARVAL CUTICLE GENE HOMOLOGOUS TO DROSOPHILA CUTICLE GENES [J].