PURIFICATION OF ACTIN BASED MOTOR PROTEIN FROM CHARA-CORALLINA

被引：56

作者：

YAMAMOTO, K

KIKUYAMA, M

SUTOHYAMAMOTO, N

KAMITSUBO, E

机构：

[1] UNIV AIR, FAC LIBERAL ARTS, BIOL LAB, MIHAMA KU, CHIBA 260, JAPAN

[2] HITOTSUBASHI UNIV, BIOL LAB, TOKYO 186, JAPAN

来源：

PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES | 1994年 / 70卷 / 10期

关键词：

CYTOPLASMIC STREAMING; CHARA CORALLINA; MOTOR PROTEIN;

D O I：

10.2183/pjab.70.175

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Actin based motor protein was purified from Chara corallina?za using high performance liquid chromatography. Sodium dodecyl sulfate gel electrophoresis showed that the molecular weight of the main band was about 230 kDa. Although the molecular weight was quite similar to that of the heavy chain of muscle myosin (myosin II), the motor protein was soluble at low ionic strength and antibody raised against the main band did not recognize smooth muscle myosin. The antibody also did not recognize the actin based motor protein from lily pollen tube. The motor protein translocated fluorescently labeled actin filaments at about 25 mu m/s in the in vitro motility assay. The MgATPase activity of the motor protein was enhanced by F-actin about 150 fold. Calcium ion concentration had little effect on both the motor activity and the actin activated MgATPase activity.

引用

页码：175 / 180

页数：6

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