Barry G. Haslett

On the nature of the polymorphism of the small subunit of ribulose-1,5-diphosphate carboxylase in the amphidiploid Nicotiana tabacum

The N-terminal amino acid sequence of the small subunit of ribulose-1,5=disphosphate carboxylase from the amphidiploidNicotiana tabacum contains two polymorphisms. From examination of the equivalent sequences in the putative parent speciesNicotiana sylvestris andtomentosiformis it is concluded that the amphidiploidNicotiana tabacum has inherited two alleles for the small subunit of ribulose diphosphate carboxylase, one from each parent species. The alleles continue to be retained and expressed. The relevance of these findings is discussed in relation to the successful adaption of the amphidiploidNicotiana tabacum to a wide range of environments.

The relationships of 8 tribes of the compositae as suggested by plastocyanin amino acid sequence data

Abstract Partial amino acid sequences of the plastocyanins from 22 members of 8 tribes of the Compositae are separated by ancestral amino acid sequence methods into 3 groups. These groups agree generally with those of previous classifications of the species from which the plastocyanins were obtained, based mainly on morphological characters, although closer relationships between the Cichorieae and Cynareae, between the Heliantheae, Senecioneae and Calenduleae and between the Astereae and Inuleae are suggested by the sequence data.

The N-terminal amino acid sequence of the small subunit of ribulose-1,5-diphosphate carboxylase fromNicotiana tabacum

The N-terminal sequence of the small subunit of Fraction I protein isolated from tobacco was investigated, using an automatic protein sequencer. The amino acid sequence of the first 21 residues is presented.

Studies on the small subunit of Fraction I protein from pisum sativum L. andvicia faba L.

We have measured the molecular weight of the small subunit of Fraction I protein from pea and broad bean by sodium dodecyl sulphate polyacrylamide gel electrophoresis, Sephadex gel-filtration and amino acid composition data. The results suggest a molecular weight of 12 000-14 500, although measurements by gel-filtration in alkali suggest a molecular weight of approximately 22 000. N-terminal amino acid sequence data and C-terminal determinations show that the protein consists of a single type of polypeptide chain, although the anomalously high molecular weight obtained on gel-filtration in alkali does not preclude the existence of the polypeptides as dimers under certain conditions.

Partial structure and properties of the ferredoxin from Rhodymenia palmata

Abstract A ferredoxin of MW 11 000 was isolated from the marine alga Rhodymenia palmata ( Palmaria palmata ). In its oxidised form the ferredoxin had absorption maxima at 276, sh 281, 328, 423 and 465 nm, and contained a single [2Fe-2S] cluster. The midpoint potential of the ferredoxin was −400 mV and it effectively mediated electron transport in NADP + -photoreduction by higher plant chloroplasts, and pyruvate decarboxylation by the phosphoroclastic system of an anacrobic bacterium. The amino acid composition was Lys 3 , His 1 , Arg 1 , Asx 12 , Thr 9 , Ser 8 , Glx 13 , Pro 4 , Gly 8 , Ala 7 , Cys 5 , Val 8 , Ile 4 , Leu 9 , Tyr 4 , Phe 2 ; tryptophan and methionine were absent from the molecule. The N -terminal amino acid region consisting of ca half the total amino acid sequence was determined using an automatic sequencer.

Comparative properties of ferredoxins from a marine and freshwater species of Porphyridium

Abstract Ferredoxins were isolated from the freshwater red alga Porphyridium aerugineut, and from Porphyridium cruentum, a related marine species. A sin

Amino acid sequence of plastocyanin from Solanum crispum using automatic methods

Abstract The complete amino acid sequence of plastocyanin of Solanum crispum L. was determined on 6 micromole protein using automatic solid-phase and spinning cup sequencer methods. Overlap between residues Lys 54 and Ile 55 was however not demonstrated. The protein consists of 99 residues.

The amino acid sequence of plastocyanin from Rumex obtusifolius

Abstract The amino acid sequence of plastocyanin from dock has been completed. It is a single polypeptide chain of 99 residues which is closely related to other plant plastocyanins. Compared to a preliminary sequence presented earlier, the completed sequence now shows two changes, at positions 53 and 92.