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Presence of two subunit types in ribulose 1,5-bisphosphate carboxylase from Thiobacillus intermedius.
J Bacteriol. 1980 Feb;141(2):652-7. doi: 10.1128/jb.141.2.652-657.1980.
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Ribulose 1,5-bisphosphate carboxylase/oxygenase from Pseudomonas oxalacticus.
J Bacteriol. 1979 Jul;139(1):287-98. doi: 10.1128/jb.139.1.287-298.1979.
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Subunit dissociation and reconstitution of ribulose-1,5-bisphosphate carboxylase from Chromatium vinosum.
Arch Biochem Biophys. 1985 Feb 1;236(2):487-96. doi: 10.1016/0003-9861(85)90651-4.
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Crystalline ribulose bisphosphate carboxylase/oxygenase of high integrity and catalytic activity from Nicotiana tabacum.
Arch Biochem Biophys. 1985 Apr;238(1):154-60. doi: 10.1016/0003-9861(85)90151-1.

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2
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75.
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Protein liganding to the activator cation of ribulosebisphosphate carboxylase.
Biochemistry. 1982 Dec 21;21(26):6669-74. doi: 10.1021/bi00269a009.
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Measurement of molecular weights by electrophoresis on SDS-acrylamide gel.
Methods Enzymol. 1972;26:3-27. doi: 10.1016/s0076-6879(72)26003-7.
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Estimation of the molecular weight of ribulose diphosphate carboxylase sub-units.
Biochem Biophys Res Commun. 1970 Jun 5;39(5):923-9. doi: 10.1016/0006-291x(70)90412-2.

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