PEPTIDES OBTAINED FROM ELASTIN BY HYDROLYSIS WITH AQUEOUS ETHANOLIC POTASSIUM HYDROXIDE

被引:18
作者
MOCZAR, M
MOCZAR, E
ROBERT, L
机构
[1] Laboratoire de Biochimie du Tissu Conjonctif (GR CNRS No. 40), Inst. Rech., Univ. Maladies Vasculaires, Fac. Mid., Univ. Paris XII, 94000, Creteil
关键词
D O I
10.3109/03008207909152322
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Elastin from bovine ligamentum nuchae was hydrolyzed with 1 M KOH in 80% ethanol at 37°C for 0.5 to 72 h. Sephadex G 100 gel filtration separated the coacervable fractions from the retarded peptides (MW: 16,000) unable to form coacervates. Their ratio changed with progressing hydrolysis. The maximal yield fo coacervable peak was obtained after hydrolysis for about 6 h, whereas after hydrolysis from 18 to 72 h, only a nonco-acervable peak was recovered. The noncoacervable Sephadex peak was eluted at an identical position after hydrolysis for 4 and 72 h with an apparent molecular weight of 16,000 dalton on polyacrylamide SDS gel electrophoresis. The noncoacervable Sephadex peaks (MW: 16,000) obtained after hydrolysis for 4 and 72 h were submitted to isoelectric focusing in Servalyt in the pH range 2.5-11. The major crosslinked peptides were refocused in the pH range 2.5-6. In the major purified crosslinked peptides, recovered after hydrolysis for 4 h, the Ala to Gly ratio (1:1) was similar to that found in elastin. The minor component lacking desmosines is rich in Ala, Pro and Gly. In the crosslinked peptides separated after hydrolysis for 72 h, the ratio of Ala to Gly is 2:1 and their desmosine content is about 2.5 times higher than in elastin. The resistance of elastin peptides to hydrolysis with ethanolic KOH appears to be related to their high Ala and Des content. © 1979 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
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页码:207 / 213
页数:7
相关论文
共 24 条
[1]   CALCIUM ION-BINDING STUDY ON ALPHA-ELASTIN [J].
ABATANGE.G ;
DAGAGORD.D ;
GARBIN, G ;
CORTIVO, R .
BIOCHIMICA ET BIOPHYSICA ACTA, 1974, 371 (02) :526-533
[2]  
ANDERSON JC, 1976, INT REV CONNECT TISS, V7, P251
[3]  
ANWAR RA, 1977, ELASTIN ELASTIC TISS, P329
[4]   ISOLATION AND CHARACTERIZATION OF A GLYCOPROTEIN FROM HUMAN THORACIC AORTA [J].
BARNES, MJ ;
PARTRIDGE, SM .
BIOCHEMICAL JOURNAL, 1968, 109 (05) :883-+
[5]   ISOLATION OF 2 PEPTIDES FROM ELASTIN [J].
CASTELLA.I ;
VOLPIN, D .
BIOCHIMICA ET BIOPHYSICA ACTA, 1974, 371 (02) :299-303
[6]   IMMUNE-RESPONSE TO PEPTIDES PRODUCED BY ENZYMATIC DIGESTION OF MICROFIBRILS AND ELASTIN OF HUMAN LUNG PARENCHYMA [J].
DARNULE, TV ;
LIKHITE, V ;
TURINO, GM ;
MANDL, I .
CONNECTIVE TISSUE RESEARCH, 1977, 5 (02) :67-73
[7]   ISOLATION AND CHARACTERIZATION OF A HIGHLY CROSSLINKED PEPTIDE FROM ELASTIN OF PORCINE AORTA [J].
DAVRIL, M ;
HAN, KK .
FEBS LETTERS, 1974, 43 (03) :331-336
[8]   ELECTROPHORETIC ANALYSIS OF MAJOR POLYPEPTIDES OF HUMAN ERYTHROCYTE MEMBRANE [J].
FAIRBANKS, G ;
STECK, TL ;
WALLACH, DFH .
BIOCHEMISTRY, 1971, 10 (13) :2606-+
[9]   ISOLATION AND CHARACTERIZATION OF CROSSLINKED PEPTIDES FROM ELASTIN [J].
FOSTER, JA ;
GRAY, WR ;
FRANZBLAU, C .
BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 303 (02) :363-369
[10]   MOLECULAR MODEL FOR ELASTIN STRUCTURE AND FUNCTION [J].
GRAY, WR ;
SANDBERG, LB ;
FOSTER, JA .
NATURE, 1973, 246 (5434) :461-466