Small subunit contacts in ribulose-1,5-bisphosphate carboxylase
- 21 February 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (4) , 665-668
- https://doi.org/10.1021/bi00597a016
Abstract
The arrangement of subunits [pea] of ribulosebisphosphate carboxylase [EC 4.1.1.39] in solution was studied by exposing the enzyme to the cross-linking agents tetranitromethane, dimethyl suberimidate and dimethyl adipimidate, and the cleavable cross-linking agent, methyl 4-mercaptobutyrimidate, followed by gel electrophoresis in the presence of dodecyl sulfate. All these agents caused the formation of dimers of the enzyme''s small subunit, independently of protein concentration. In addition, trimers and tetramers of small subunit were detected in the mercaptobutyrimidate-treated enzyme. The data show that small subunits are closely paired in the native enzyme and may be in layers of 4, or a ring of 8.This publication has 2 references indexed in Scilit:
- Ribulose Bisphosphate Carboxylase: A Two-Layered, Square-Shaped Molecule of Symmetry 422Science, 1977
- Structure of ribulose-1,5-bisphosphate carboxylase-oxygenase: Form III crystalsProceedings of the National Academy of Sciences, 1977