Identification of haem-proteins in thylakoid polypeptide patterns of barley [haem associated peroxidase activity, SDS-polyacrylamide gel electrophoresis, lithium dodecyl sulfate, LiDS-polyacrylamide gel electrophoresis, cytochromes]
1980
Hoeyer-Hansen, G.
Thylakoid polypeptides from barley were separated by polyacrylamide gel electophoresis by use of either SDS or LiDS as the detergent. Staining of either gel-type with 3,3',5,5'-tetramethylbenzidine-H(,2)O(,2) revealed two barley polypeptides with peroxidase activity. The same two polypeptides were shown to incorporate [('14)C]-delta-aminolaevulinic acid, identifying haem as their prosthetic group. The haem-protein with a molecular weight of 33,000 is cytochrome f and that with a molecular weight of 20,000 is suggested to be a subunit of cytochrome b(,6). The two polypeptides are also present in citoplast membranes, which from prior spectroscopic evidence are known to contain cytochromes f and b(,6).
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