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1. Molecular Weight and Quaternary Structure of Yeast L-Lactase Dehydrogenase (Cytochrome b2).

Author

Jacq, C. and Lederer, F.

Subjects
DEHYDROGENASES, MOLECULAR weights, AMINO acids, CYTOCHROME c, BIOLOGY, CHEMISTRY, BIOCHEMISTRY
Abstract

Amino acid analyses of L-lactate dehydrogenase from baker's show that the minimum molecular weight (53 000 daltons) of the protein is much lower than found in the literature (80 000). This result, combined with those reported in the following papers, leads to a revision of the dimeric model generally accepted for cytochrome b2 [ABSTRACT FROM AUTHOR]

Published
1970
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2. Molecular Weight and Quaternary Structure of Yeast L-Lactase Dehydrogenase (Cytochrome b2).

Author

Jacq, C. and Lederer, F.

Subjects
*DEHYDROGENASES, *MOLECULAR weights, *AMINO acids, *CYTOCHROME c, *BIOLOGY, *CHEMISTRY, *BIOCHEMISTRY
Abstract

Amino acid analyses of L-lactate dehydrogenase from baker's show that the minimum molecular weight (53 000 daltons) of the protein is much lower than found in the literature (80 000). This result, combined with those reported in the following papers, leads to a revision of the dimeric model generally accepted for cytochrome b2 [ABSTRACT FROM AUTHOR]

Published
1970
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3. On the Presence of a Non-Trimethylated iso-1 Cytochrome <em>c</em> in a Wild-Type Strain of <em>Saccharomyces cerevisiae</em>.

Author

Foucher, Marcelle, Verdière, Jacqueline, Lederer, Florence, and Slonimski, Piotr P.

Subjects
SACCHAROMYCES cerevisiae, CYTOCHROME c, ION exchange chromatography, BIOLOGY, CHEMISTRY, BIOCHEMISTRY
Abstract

Ion-exchange chromatography of the total cytochrome c extracted from a wild-type laboratory strain of Saccharomyces cerevisiae shows the presence of two minor cytochrome c peaks, besides the already known iso-1 and iso-2 cytochromes c. Their amino acid composition is very similar to that of iso-1, but one of them lacks the ε-N-trimethylated lysine residue characteristic of yeast cytochromes c, thus excluding, at least for this peak, an artifactual origin. [ABSTRACT FROM AUTHOR]

Published
1972
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4. The amino acid sequence of cytochrome c from Helix aspersa Müller (garden snail)

Author

R. P. S. Jefferies, Michael Richardson, R. H. Brown, Donald Boulter, and J. A. M. Ramshaw

Subjects
History, Snails, Cytochrome c Group, Snail, Mitochondrion, Education, biology.animal, Animals, Amino Acid Sequence, Peptide sequence, chemistry.chemical_classification, biology, Cytochrome c, Helix (gastropod), myr, Articles, biology.organism_classification, Biological Evolution, Computer Science Applications, Amino acid, Mitochondria, chemistry, Biochemistry, biology.protein, Garden Snail, Peptides
Abstract

The amino acid sequence of a snail cytochrome c has been determined. The molecule consists of a single polypeptide chain of 104 residues, and is homologous with other mitochondrial cytochromes c. Unlike the cytochromes c from vertebrates, there is no acetyl blocking group at the N-terminus. A change in an otherwise invariant position has been observed in position 87. Comparison with amino acid sequences of cytochromes c from other sources indicates that the point of divergence of the molluscs and the vertebrates in evolutionary time was 720 million years ago. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50009 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972), 126, 5.

Published
1972