Reference "Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays: amino-acid sequence of the small subunit"

Reference ID

7328

Title

Ribulose-1,5-bisphosphate carboxylase/oxygenase from Zea mays: amino-acid sequence of the small subunit

Source

Biological chemistry Hoppe-Seyler, 1988, vol. 369, pp. 609-615

Authors (3)

Ren-L	Salnikow-J
Vater-J

Abstract

The amino-acid sequence of the small subunit of ribulose-1,5-bisphosphate
carboxylase/oxygenase from Zea mays has been determined by alignment of peptides
generated by digestion with trypsin, chymotrypsin, staphylococcal protease and
thermolysin. The protein-chemically determined structure is in complete
agreement with the nucleotide-derived sequence as published recently (Matsuoka
et al. (1987) J. Biochem. 102, 673-676), but in addition possesses, however,
sixteen experimentally verified dimorphies at various positions and possibly
nine more for which evidence is tentatively pointing to two (or more) different
expressed nuclear genes for the small subunit. These protein dimorphies
represent a protein family corresponding to a gene family, the components of
which have not been separated. The closest homologous polypeptide is the small
subunit from wheat.