COMPLETE DETERMINATION OF DISULFIDE BONDS LOCALIZED WITHIN THE SHORT CONSENSUS REPEAT UNITS OF DECAY ACCELERATING FACTOR (CD55-ANTIGEN)

被引：17

作者：

NAKANO, Y

SUMIDA, K

KIKUTA, N

MIURA, NH

TOBE, T

TOMITA, M

机构：

[1] Department of Physiological Chemistry, School of Pharmaceutical Sciences, Showa University, Shinagawa-ku, Tokyo

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1116卷 / 03期

关键词：

DECAY-ACCELERATING FACTOR; SHORT CONSENSUS REPEAT; DISULFIDE BOND; HPLC;

D O I：

10.1016/0304-4165(92)90016-N

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：

Decay accelerating factor (DAF) has 4 SCR (short consensus repeat) units. Each SCR unit consists of approx. 60 amino acids characterized by having four conserved cysteine residues and several other highly conserved residues which include proline, tryptophan, tyrosine/phenylalanine and glycine. To determine the disulfide-bonding pattern, we used the urine form of DAF. After thermolysin and trypsin digestion, we isolated seven disulfide-linked peptides by HPLC purification. Because all of the cysteine residues are disulfide-bonded, DAF should contain eight disulfide bonds. After subtilisin and trypsin digestion, we isolated the eighth disulfide-bonded peptides by HPLC purification. From sequence analyses of these peptides, we could identify all disulfide bonds in the 4 SCR units of DAF as being between the first and the third and between the second and the fourth half-cystines within each SCR unit.

引用

页码：235 / 240

页数：6

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