Isolation of active ribulose-1,5-bisphosphate carboxylase from cotton leaves of Gossypium hirsutum and G. barbadense L. species

Authors

  • I. Ph. Karpilova Institute of Soil Science and Photosynthesis RAS 2, Istitutskaya Str., Pushchino, Moscow Region, Russian Federation, 142290 Author
  • I. M. Sokolova Institute of Experimental Biology of Plants, Academy of Sciences of the Republic of Uzbekistan Uzbekistan Author
  • S. M. Gaziyants Institute of Soil Science and Photosynthesis RAS 2, Istitutskaya Str., Pushchino, Moscow Region, Russian Federation, 142290 Author

DOI:

https://doi.org/10.7124/bc.00032B

Abstract

A rapid method of isolation of ribulose-1,5-bisphosphate carboxylase from cotton leaves is offered. Definite complex of additional substances completely bio-cades the polyphenoles and allows to obtain high level of common and specific activities of Rubisco isolated from adult cotton leaves with high content of phenolic substances. Method is useful for the comparative analysis of the examples seria and may be used for the genetic and evolutional investigations.

References

Ellis RJ. The most abundant protein in the world. Trends Bioche Sci. 1979;4(11):241–4.

Quayle TJ, Katterman FR, Jensen RG. Isolation of active ribulose 1,5-bisphosphate carboxylase from glanded cotton (G. hirsutum). Physiol Plant. 1980;50(3):233–6.

Karpilova IF, Romanova AK, Ragimova NG, Pachepskaya LB. Effect of temperature on ribulose bisphosphate carboxylase of clover leaves in early ontogeny. Fiziologiia rasteniy. 1988; 35(1): 41-50.

Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54.

King EE. Extraction of cotton leaf enzymes with borate. Phytochemistry. 1971;10(10):2337–41.

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Published

1992-07-20

Issue

Vol. 8 No. 4 (1992)

Section

Structure and Function of Biopolymers