CHARACTERIZATION OF GLYCYRRHIZIN-BINDING PROTEIN-KINASE FROM THE CRUDE MEMBRANE-FRACTION OF RAT-LIVER

被引:20
作者
ISHIKAWA, A
KANAMARU, R
WAKUI, A
KANNO, S
OHTSUKI, K
机构
[1] KITASATO UNIV,SCH HYG SCI,DEPT BIOSCI,SAGAMIHARA,KANAGAWA 228,JAPAN
[2] TOHOKU UNIV,INST CANC,DEPT CLIN CANC CHEMOTHERAPY,SENDAI,MIYAGI 980,JAPAN
关键词
D O I
10.1016/0006-291X(90)90605-M
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
Using GL-affinity column chromatography, a casein phosphorylating protein kinase was purified selectively from the crude membrane fraction of rat liver. The biochemical characteristics of the purified kinase (approximately Mr 210 kDa) are very similar to those reported for polypeptide-dependent protein kinase (kinase P). Moreover, low doses of GL selectively inhibit phosphorylation of Mr 35-36 kDa polypeptides (which are cross-reacted with anti-lipocortins I and II) by the kinase invitro. These results suggest that the anti-inflammatory activity of GL may involve the impairment of the physiological functions of lipocortins through their specific modification by the kinase at the cell membrane level. © 1990.
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收藏
页码:876 / 882
页数:7
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