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Rapid isolation of genes from bacterial lambda libraries by direct polymerase chain reaction screening
Authors:Hugh G Griffin  Kerry J I'Anson  Michael J Gasson
Institution:Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo, Japan
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 .
Keywords:Ribulose bis-phosphate carboxylase  L2 RubisCO              Hydrogenovibrio marinus
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