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High specific activity ribulose 1,5-bisphosphate carboxylase-oxygenase fromNicotiana tabacum

✍ Scribed by James T. Bahr; Sarjit Johal; Malcolm Capel; Don P. Bourque

Publisher
Springer
Year
1981
Tongue
English
Weight
418 KB
Volume
2
Category
Article
ISSN
0166-8595

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✦ Synopsis

Ribulose 1,5-bisphosphate carboxylase (EC.4.1.1.39) has been obtained from Nicotiana tabacum leaf homogenates with specific activites from 0.5 to 0.8 Β΅mol CO2 fixed (mg protein min)(-1). These activities are reconciled with much lower, previously reported activities. The results suggest that if the tobacco enzyme is assayed under optimum conditions there is little difference in the intrinsic specific activities of tobacco and spinach ribulose 1,5-bisphosphate carboxylase. Several factors affecting activity measurements were examined.

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