Structural and immunoelectrophoretic comparison of soluble and particulate ribulose bisphosphate carboxylases from the cyanobacterium Chlorogloeopsis fritschii |
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Authors: | T Lanaras G A Codd |
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Institution: | (1) Department of Biological Sciences, University of Dundee, DD1 4HN Dundee, UK |
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Abstract: | The soluble and particulate (carboxysomal) forms of ribulose 1,5-bisphosphate (RuBP) carboxylase from the cyanobacterium Chlorogloeopsis fritschii have been purified separately. A molecular weight of 520,000 was found in each case. Large (L, 53,000) and small (S, 13,000) subunits were obtained after dissociation, indicating a L8S8 quaternary structure for the enzyme from both sources. The L and S subunits are identical in molecular weight to the major polypeptides present in isolated dissociated C. fritschii polyhedral bodies (carboxysomes). Occasionally an additional polypeptide (mol. wt. 45,000) was found after dissociation of the soluble enzyme only, although the possibility that this may be due to proteolysis is not discounted. Immunochemical identity between the purified soluble and carboxysomal RuBP carboxylases was indicated by tandem-crossed and rocket immunoelectrophoresis.Abbreviations PAGE
polyacrylamide gel electrophoresis
- SDS
sodium dodecyl-sulphate
- RuBP
D-ribulose 1,5-bisphosphate
- TCA
trichloroacetic acid
- LTIB
low Tris isolation buffer
- HTIB
high Tris isolation buffer
- CIE
crossed immunoelectrophoresis
- TCIE
tandem-crossed immunoelectrophoresis
- RIE
rocket immunoelectrophoresis |
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Keywords: | Chlorogloeopsis fritschii Ribulose bisphosphate carboxylase Polyhedral bodies Carboxysomes |
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