Rapid isolation of genes from bacterial lambda libraries by direct polymerase chain reaction screening |
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Authors: | Hugh G Griffin Kerry J I'Anson Michael J Gasson |
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Institution: | Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, Japan |
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Abstract: | Abstract Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) was purified from an obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus MH-110. The protein has a M r value of approximately 110 000, and is composed of two identical subunits of 55 000. To our knowledge, the existence of L2-form RubisCO in a chemolithoautotrophic bacterium is first reported in this paper. The N-terminal amino acid sequence determination of the purified enzyme showed high homology with those of the L2-form RubisCO of Rhodospirillum rubrum and the L x -form RubisCO from Rhodobacter sphaeroides . |
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Keywords: | Ribulose bis-phosphate carboxylase L2 RubisCO Hydrogenovibrio marinus |
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