AMINO-ACID-SEQUENCE ANALYSIS OF HUMAN S100A7 (PSORIASIN) BY TANDEM MASS-SPECTROMETRY

被引：14

作者：

BURGISSER, DM

SIEGENTHALER, G

KUSTER, T

HELLMAN, U

HUNZIKER, P

BIRCHLER, N

HEIZMANN, CW

机构：

[1] UNIV ZURICH,DEPT PEDIAT,DIV CLIN CHEM,CH-8032 ZURICH,SWITZERLAND

[2] HOP CANTONAL UNIV GENEVA,DERMATOL CLIN,CH-1211 GENEVA 14,SWITZERLAND

[3] LUDWIG INST CANC RES,S-75124 UPPSALA,SWEDEN

[4] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 217卷 / 01期

关键词：

D O I：

10.1006/bbrc.1995.2772

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 Ca2+-binding proteins regulate a number of cellular and extracellular activities and deregulations of S100 gene expression are associated with several human diseases. For example, S100A7 is upregulated in psoriatic skin, implicating a link with psoriasis, a chronic inflammatory dermatosis. We purified human S100A7 and determined its protein sequence by tandem mass spectrometry and Edman microsequence analysis. Interestingly, a sequence comparison of S100A7 with all known human S100 proteins showed that S100A7 is the most divergent of all S100 proteins. (C) 1995 Academic Press, Inc.

引用

页码：257 / 263

页数：7

共 12 条

[1] PROTEIN-SEQUENCE DETERMINATION BY ESI-MS AND LSI-MS TANDEM MASS-SPECTROMETRY - PARVALBUMIN PRIMARY STRUCTURES FROM CAT, GERBIL AND MONKEY SKELETAL-MUSCLE [J].