Ribulose Bisphosphate Carboxylase from Three Chlorophyll c-Containing Algae

Autor:	Schmidt Gw, Kirchman Dl, Hodson Re, Plumley Fg
Rok vydání:	1986
Předmět:	biology Physiology Ribulose Protein subunit RuBisCO Chlorophyll c Chlamydomonas reinhardtii Plant Science biology.organism_classification chemistry.chemical_compound Cryptomonas Isoelectric point Biochemistry chemistry Chlorophyll Genetics biology.protein
Zdroj:	Plant Physiology. 80:685-691
ISSN:	1532-2548 0032-0889
DOI:	10.1104/pp.80.3.685
Popis:	Distinctive properties are identified in the molecular structure of ribulose, 1,5-bisphosphate carboxylase/oxygenase (RuBPCase) in chlorophyll c-containing algae (i.e., chromophytes). Using purified enzyme from Cryptomonas sp., Coccolithophora sp., and Cylindrotheca fusiformis, we have determined that the RuBPCase holoenzyme of each species has a molecular weight, subunit composition, and isoelectric points of its subunits similar to the purified enzymes from pea and Chlamydomonas reinhardtii. The large subunits from chromophytes exhibit microheterogeneity in their isoelectric points, whereas two to four well-resolved isoelectric variants of the small subunit were observed in each RuBPCase preparation. In spite of the high degree of similarity in terms of physical properties, both the small and large RuBPCase subunits of the chromophytes are structurally different from those of chlorophytes; immunological studies demonstrate that RuBPCase subunits of these two groups have few antigenic determinants in common.
Databáze:	OpenAIRE
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