DIVERSE EFFECTS OF POLYBASIC AMINO-ACIDS, HEPARIN AND IONIC-STRENGTH ON THE PHOSPHORYLATION OF VARIOUS SUBSTRATES BY CYTOSOLIC PROTEIN TYROSINE KINASE FROM PORCINE SPLEEN

被引:4
作者
ASAHI, M [1 ]
TANIGUCHI, T [1 ]
SAKAI, K [1 ]
NAKAMURA, S [1 ]
YAMAMURA, H [1 ]
机构
[1] FUKUI MED SCH,DEPT BIOCHEM,FUKUI 91011,JAPAN
来源
INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1990年 / 22卷 / 06期
关键词
D O I
10.1016/0020-711X(90)90041-Z
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
1. 1. Effects of poly-basic amino acids, heparin and ionic strength on the activity of cytosolic protein-tyrosine kinase from porcine spleen (CPTK-40) have been studied. 2. 2. Both polylysine and polyarginine stimulated the phosphorylation of [Val5]angiotensin II and Eii|G1 (synthetic peptide of EDAEYAARRRG), but could neither stimulate nor inhibit the phosphorylation of random copolymers; poly(EY)4:1 and poly(EAY)6:3:1. 3. 3. Heparin stimulated the phosphorylation of poly(EY)4:1 by 2.5-fold, however, it inhibited those of E11,G1, poly(EAY)6:3:1, casein and H2B histone. 4. 4. Elevation of ionic strength of either NaCl, KC1 or (NH4)2SO4 stimulated the phosphorylation of poly(EY)4:1 >5-fold, but inhibited those of casein, tubulin. H2B histone, EiiGi and poly(EAY)6:3:1. 5. 5. These effectors did not change the Km for substrates but increased the Vmax. 6. 6. These results suggest that the effects of poly-basic amino acids, heparin and ionic strength on the activity of CPTK-40 are mainly on the substrates employed rather than on the enzyme itself. © 1990.
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页码:635 / 640
页数:6
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