THE CALMODULIN AND F-ACTIN BINDING-SITES OF SMOOTH-MUSCLE CALDESMON LIE IN THE CARBOXYL-TERMINAL DOMAIN WHEREAS THE MOLECULAR-WEIGHT HETEROGENEITY LIES IN THE MIDDLE OF THE MOLECULE

被引：0
|
作者：
RISEMAN, VM [1 ]
LYNCH, WP [1 ]
NEFSKY, B [1 ]
BRETSCHER, A [1 ]
机构：
[1] CORNELL UNIV, BIOCHEM MOLEC & CELL BIOL SECT, ITHACA, NY 14853 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 1989年 / 264卷 / 05期
关键词：
D O I：
暂无
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：
引用
收藏
页码：2869 / 2875
页数：7
相关论文
共 3 条
  • [1] Fluorescence studies of the carboxyl-terminal domain of smooth muscle calponin - Effects of F-actin and salts
    Bartegi, A
    Roustan, C
    Kassab, R
    Fattoum, A
    EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 262 (02): : 335 - 341
  • [2] PRECISE IDENTIFICATION OF THE REGULATORY F-ACTIN-BINDING AND CALMODULIN-BINDING SEQUENCES IN THE 10-KDA CARBOXYL-TERMINAL DOMAIN OF CALDESMON
    MEZGUELDI, M
    DERANCOURT, J
    CALAS, B
    KASSAB, R
    FATTOUM, A
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1994, 269 (17) : 12824 - 12832
  • [3] PROTEOLYTIC DISSECTION OF SMOOTH-MUSCLE CALDESMON INTO FRAGMENTS THAT RETAIN F-ACTIN, CA-21-CALMODULIN AND TROPOMYOSIN BINDING ACTIVITIES
    RISEMAN, VM
    BRETSCHER, A
    JOURNAL OF CELL BIOLOGY, 1986, 103 (05): : A536 - A536
1