Arid
DOI10.2172/1164812
报告编号DOE-USDA--ER20268
来源IDOSTI_ID: 1164812
Consequences of altering rubisco regulation
Salvucci, Michael [US Dept. of Agriculture (USDA)., Ames, IA (United States)]
英文摘要Research examined the thermal stability and propensity for aggregation of wild type and the C- and N-terminally modified forms of activase to determine if loss of activity under heat stress is dependent on protein aggregation. The results showed that 1) loss of activity at high temperature is independent of aggregation; 2) activase with both C- and N-terminal S-Tags are more susceptible to aggregation than wild type activase, 3) aggregation is highly dependent on the concentration of Mg2+ and 4) the ATP analog, ATPgammaS, protects against both thermal inactivation and aggregation.
出版年2013
报告类型Technical Report
语种英语
国家美国
来源学科分类99 GENERAL AND MISCELLANEOUS Photosynthesis ; Activase ; Rubisco ; Arabidopsis
URLhttp://www.osti.gov/scitech/servlets/purl/1164812
资源类型科技报告
条目标识符http://119.78.100.177/qdio/handle/2XILL650/270886
推荐引用方式
GB/T 7714
Salvucci, Michael [US Dept. of Agriculture . Consequences of altering rubisco regulation,2013.
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