DETERMINATION OF THE COVALENT STRUCTURE OF AN N-TERMINALLY AND C-TERMINALLY BLOCKED GLYCOPROTEIN FROM ENDOCUTICLE OF LOCUSTA-MIGRATORIA - COMBINED USE OF PLASMA DESORPTION MASS-SPECTROMETRY AND EDMAN DEGRADATION TO STUDY POSTTRANSLATIONALLY MODIFIED PROTEINS

被引:57
作者
TALBO, G
HOJRUP, P
RAHBEKNIELSEN, H
ANDERSEN, SO
ROEPSTORFF, P
机构
[1] ODENSE UNIV,DEPT MOLEC BIOL,CAMPUSVEJ 55,DK-5230 ODENSE,DENMARK
[2] UNIV COPENHAGEN,DEPT BIOL CHEM A,DK-1168 COPENHAGEN,DENMARK
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 195卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1991.tb15730.x
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 complete structure of a protein isolated from endocuticle of sexually mature locusts, Locusta migratoria, has been determined by a combination of automatic Edman degradation and plasma desorption mass spectrometry. The protein is extensively post-translationally modified. The N-terminal is 5-oxoproline (pyroglutamic acid) and the C-terminal proline residue is amidated. Furthermore, the protein is glycosylated by a single N-acetylgalactosamine residue at one, two or three threonines. The N-terminal sequence was obtained by analysing the N-acetylated N,O-permethylated derivative using plasma desorption mass spectrometry. The position and type of carbohydrate were determined by combining an HPLC-based carbohydrate analysis with the peak pattern of the phenylthiohydantoin derivative in automatic sequencing and with mass information on peptides. The protein has pronounced similarity to cuticular proteins from larvae of diptera and lepidoptera, but only slight resemblance to the previously sequenced locust exocuticular proteins. This indicates a similarity between soft larval cuticles and locust endocuticle, a similarity which may extend to their mechanical properties.
引用
收藏
页码:495 / 504
页数:10
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