期刊论文详细信息
FEBS Letters
Differences in polypeptide composition and enzyme activity between cold‐stable and cold‐labile microtubules and study of microtubule alkaline phosphatase activity
Hesketh, J.E.1 
[1] Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB, Scotland
关键词: Microtubule;    Cold stability;    Microtubule-associated protein;    SDS-gel electrophoresis;    Alkaline phosphatase;    Zinc;   
DOI  :  10.1016/0014-5793(84)80341-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Cold-stable and cold-labile microtubules were prepared by two cycles of assembly and disassembly and two periods of exposure to cold. The cold-labile preparations were shown to contain a higher proportion of a high molecular mass microtubule-associated protein (MAP 2) than cold-stable preparations. The cold-stable preparations showed a much higher alkaline phosphatase activity. Stimulation of microtubule assembly by zinc led to increases in both cold stability and alkaline phosphatase activity.

【 授权许可】

Unknown   

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