RIBONUCLEASE-ACTIVITY AND SUBSTRATE PREFERENCE OF HUMAN EOSINOPHIL CATIONIC PROTEIN (ECP)

被引：38

作者：

SORRENTINO, S ^{[1
]}

GLITZ, DG ^{[1
]}

机构：

[1] UNIV CALIF LOS ANGELES,SCH MED,DEPT BIOL CHEM,LOS ANGELES,CA 90024

来源：

FEBS LETTERS | 1991年 / 288卷 / 1-2期

关键词：

EOSINOPHIL PROTEIN; HELMINTHOTOXIN; NEUROTOXIN; RIBONUCLEASE ACTIVITY; RIBONUCLEASE SUPERFAMILY;

D O I：

10.1016/0014-5793(91)80994-E

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 eosinophil cationic protein (ECP), a potent helminthotoxin with considerable neurotoxic activity, was recently shown to also have ribonucleolytic activity. In this work the substrate preference of ECP ribonuclease action was studied in detail. With single-stranded RNA or synthetic polyribonucleotide substrates ECP showed significant but low activity, 70- to 200-fold less than that of bovine RNase A. ECP hydrolyzed RNA more rapidly than it did any synthetic polynucleotide. Poly(U) was degraded more rapidly than poly(C), and poly(A) and double-stranded substrates were extremely resistant. Defined low molecular weight substrates in the form of the 16 dinucleoside phosphates (NpN') and uridine and cytidine 2', 3'-cyclic phosphates were tested, and none showed hydrolysis by ECP at a significant rate. The results link ECP ribonucleolytic activity to the 'non-secretory' liver-type enzymes rather than to the 'secretory' pancreatic-type RNases.

引用

页码：23 / 26

页数：4

共 33 条

[1]

BARKER RL, 1989, J IMMUNOL, V143, P952

[2] AMINO-ACID SEQUENCE OF THE NONSECRETORY RIBONUCLEASE OF HUMAN-URINE [J].

BEINTEMA, JJ ;

HOFSTEENGE, J ;

IWAMA, M ;

MORITA, T ;

OHGI, K ;

IRIE, M ;

SUGIYAMA, RH ;

SCHIEVEN, GL ;

DEKKER, CA ;

GLITZ, DG .

BIOCHEMISTRY, 1988, 27 (12) :4530-4538

[3]

BEINTEMA JJ, 1988, BIOCHEM J, V255, P501

[4] THE AMINO-ACID-SEQUENCE OF HUMAN PANCREATIC RIBONUCLEASE [J].

BEINTEMA, JJ ;

WIETZES, P ;

WEICKMANN, JL ;

GLITZ, DG .

ANALYTICAL BIOCHEMISTRY, 1984, 136 (01) :48-64

[5] PRESENCE OF A BASIC AMINO-ACID RESIDUE AT EITHER POSITION-66 OR POSITION-122 IS A CONDITION FOR ENZYMIC ACTIVITY IN THE RIBONUCLEASE SUPERFAMILY [J].

BEINTEMA, JJ .

FEBS LETTERS, 1989, 254 (1-2) :1-4

[6]

BLACKBURN P, 1977, J BIOL CHEM, V252, P5904

[7]

CARSANA A, 1988, NUCLEIC ACIDS RES, V16, P5591

[8] SPECTROPHOTOMETRIC ASSAY OF BOVINE PANCREATIC RIBONUCLEASE BY THE USE OF CYTIDINE 2'-3'-PHOSPHATE [J].

CROOK, EM ;

MATHIAS, AP ;

RABIN, BR .

BIOCHEMICAL JOURNAL, 1960, 74 :234-238

[9] A RIBONUCLEASE FROM HUMAN SEMINAL PLASMA ACTIVE ON DOUBLE-STRANDED-RNA [J].

DEPRISCO, R ;

SORRENTINO, S ;

LEONE, E ;

LIBONATI, M .

BIOCHIMICA ET BIOPHYSICA ACTA, 1984, 788 (03) :356-363

[10]

ELSON M, 1976, BIOCHEMISTRY-US, V14, P1471

← 1 2 3 4 →