scholarly journals The amino acid sequence of cytochrome c from the locust, Schistocerca gregaria Forskal

1977 ◽  
Vol 163 (2) ◽  
pp. 333-338 ◽  
Author(s):  
A Lyddiatt ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Schistocerca Gregaria ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Single Polypeptide ◽  
Taxonomic Groups ◽  
Mitochondrial Cytochromes

The amino acid sequence of locust cytochrome c was determined, although the overlap between chymotryptic and tryptic peptides at residues tyrosine-97 and leucine-98 was not observed, owing to an anomalous tryptic break duplicating the chymotryptic digestion. The molecule consists of a single polypeptide chain of 107 residues, homologous with other mitochondrial cytochromes c. In common with other known insect cytochromes c, it possesses a non-acetylated, four-residue tail at the N-terminus relative to glycine-1 of the standard alignment. A molecular phylogeny for 17 species was constructed relating the cytochrome c molecules of Schistocerca gregaria and other invertebrates with those of representative taxonomic groups. Experimental details are given in a supplementary paper deposited as Supplementary Publication SUP 50077 (24 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can obtained on the terms indicated in Biochem. J. (1977) 161, 1.

scholarly journals The amino acid sequence of cytochrome c from Helix aspersa Müller (garden snail)

1972 ◽  
Vol 128 (4) ◽  
pp. 971-974 ◽  
Author(s):  
R. H. Brown ◽  
M. Richardson ◽  
D. Boulter ◽  
J. A. M. Ramshaw ◽  
R. P. S. Jefferies
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Blocking Group ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Polypeptide ◽  
Mitochondrial Cytochromes

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.

scholarly journals The amino acid sequence of cytochrome c′ from the purple sulphur bacterium Chromatium vinosum

1979 ◽  
Vol 177 (3) ◽  
pp. 819-823 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Rhodospirillum Rubrum ◽  
Chromatium Vinosum ◽  
Peptide Sequence ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Purple Sulphur Bacterium

An amino acid sequence is proposed for the cytochrome c′ from the photosynthetic purple sulphur bacterium Chromatium vinosum strain D. It is single polypeptide chain of 131 residues, with haem-attachment cysteine residues at positions 121 and 124. The results discredit an earlier report [Dus, Bartsch & Kamen (1962) J. Biol. Chem 237, 3083–3093] of a di-haem peptide sequence from this protein. The sequence belongs to the same class as the published Alcal!igenes and Rhodospirillum rubrum cytochrome c′ squences, but the resemblance is not close. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50,093 (15 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1978) 169, 5.

scholarly journals The amino acid sequence of the dihaem cytochrome c4 from the bacterium Azotobacter vinelandii

1984 ◽  
Vol 222 (1) ◽  
pp. 217-227 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
K Melis ◽  
C D Stout
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Azotobacter Vinelandii ◽  
Cysteine Residues ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Cytochromes C ◽  
Single Polypeptide

An amino acid sequence is proposed for the cytochrome c4 from the bacterium Azotobacter vinelandii strain OP. It is a single polypeptide chain of 190 residues, with two sets of haem-attachment cysteine residues at positions 14/17 and 119/122. Proteins with similar sequences are also present in denitrifying pseudomonads. There is similarity in sequence between the two halves of the cytochrome c4 molecule, and each half also shows similarity to the sequences of certain monohaem cytochromes c isolated from organisms that are not obviously closely related to A. vinelandii. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50125 (17 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus

1986 ◽  
Vol 233 (2) ◽  
pp. 333-337 ◽  
Author(s):  
R P Ambler ◽  
H Dalton ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Methylococcus Capsulatus ◽  
Methionine Residue ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of the cytochrome c-555 from the obligate methanotroph Methylococcus capsulatus strain Bath (N.C.I.B. 11132) was determined. It is a single polypeptide chain of 96 residues, binding a haem group through the cysteine residues at positions 19 and 22, and the only methionine residue is a position 59. The sequence does not closely resemble that of any other cytochrome c that has yet been characterized. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50131 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals The amino acid sequence of cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015

1973 ◽  
Vol 135 (4) ◽  
pp. 751-758 ◽  
Author(s):  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Attachment Site ◽  
Photosynthetic Bacterium ◽  
Chromatium Vinosum ◽  
British Library ◽  
Pseudomonas Denitrificans ◽  
Single Polypeptide Chain ◽  
C Terminus

The amino acid sequence of the cytochrome c′ from Alcaligenes sp. N.C.I.B. 11015 (Iwasaki's ‘Pseudomonas denitrificans’) has been determined. This organism is the only non-photosynthetic bacterium in which the protein has been found. The protein consists of a single polypeptide chain of 127 residues, with a single haem covalently attached to two cysteines. Unlike normal cytochromes c, the haem attachment site is very close to the C-terminus. The amino acid sequence around the haem attachment site is very similar to that of Chromatium vinosum D cytochrome c′. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50022 at the British Library (Lending Division), (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

scholarly journals The amino acid sequence of cytochrome c of Fagopyrum esculentum Moench (buckwheat) and Brassica oleracea L. (cauliflower)

1971 ◽  
Vol 124 (4) ◽  
pp. 783-785 ◽  
Author(s):  
E. W. Thompson ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Brassica Oleracea ◽  
Amino Acid Sequences ◽  
Cytochromes C ◽  
Lending Library ◽  
Fagopyrum Esculentum Moench ◽  
Mitochondrial Cytochromes ◽  
Brassica Oleracea L

The amino acid sequences of buckwheat and cauliflower cytochromes c were determined on 1½μmol and 1μmol of protein respectively. The molecules consist of 111 residues and are homologous with other plant mitochondrial cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 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. (1971), 121, 7.

scholarly journals The amino acid sequence of cytochrome c from Spinacea oleracea L. (spinach)

1973 ◽  
Vol 131 (2) ◽  
pp. 253-256 ◽  
Author(s):  
R. H. Brown ◽  
M. Richardson ◽  
R. Scogin ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
Spinacea Oleracea ◽  
Cytochromes C ◽  
Lending Library ◽  
Mitochondrial Cytochromes

The amino acid sequence of spinach (Spinacea oleracea L., var. Monster Viroflay) cytochrome c was determined on 1μmol of protein. The molecule consists of 111 residues and is homologous with other mitochondrial cytochromes c. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50013, 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. (1973), 131, 5.

The Amino Acid Sequence of Cytochrome c-553 from the Chrysophycean Alga Monochrysis lutheri

1972 ◽  
Vol 50 (12) ◽  
pp. 1311-1325 ◽  
Author(s):  
M. V. Laycock
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Photosynthetic Apparatus ◽  
Amino Acid Residues ◽  
Unicellular Alga ◽  
Electron Carrier ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of cytochrome c-553, an electron carrier in the photosynthetic apparatus of the unicellular alga Monochrysis lutheri, has been determined. The protein consists of a single polypeptide chain of 83 amino acid residues. The sequence shows homology with mitochondrial cytochrome c at each end of the chain. The N-terminal glycine is not acetylated and corresponds to position 1 of mammalian cytochrome c when the cysteine residues of the two proteins are aligned.

scholarly journals The amino acid sequence of plastocyanin from French bean (Phaseolus vulgaris)

1974 ◽  
Vol 143 (3) ◽  
pp. 691-701 ◽  
Author(s):  
P. R. Milne ◽  
J. R. E. Wells ◽  
R. P. Ambler
Keyword(s):  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Amino Acid Sequence ◽  
French Bean ◽  
British Library ◽  
Single Polypeptide Chain ◽  
Unicellular Green Alga ◽  
Green Alga Chlorella ◽  
Lending Library ◽  
Single Polypeptide

The amino acid sequence of the plastocyanin from French bean (Phaseolus vulgaris) was determined. The protein consists of a single polypeptide chain of 99 residues, and the sequence was determined by characterization of CNBr, tryptic, chymotryptic and thermolysin peptides. When the sequence is compared with that from the plastocyanin of the unicellular green alga Chlorella fusca, the French-bean protein shows the deletion of the N-terminal residue, a two residue insertion and 53 identical residues. Detailed evidence for the sequence of the protein has been deposited as Supplementary Publication SUP 50037 (16pp., 1 microfiche) at the British Library (Lending Division) (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

scholarly journals The amino acid sequence of cytochrome c from Cucurbita maxima L. (pumpkin)

1971 ◽  
Vol 124 (4) ◽  
pp. 779-781 ◽  
Author(s):  
E. W. Thompson ◽  
M. Richardson ◽  
D. Boulter
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Science And Technology ◽  
Cucurbita Maxima ◽  
Cytochromes C ◽  
Lending Library ◽  
Mitochondrial Cytochromes

The amino acid sequence of pumpkin cytochrome c was determined on 2μmol of protein. Some evidence was found for the occurrence of two forms of cytochrome c, whose sequences differed in three positions. Pumpkin cytochrome c consists of 111 residues and is homologous with mitochondrial cytochromes c from other plants. Experimental details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50005 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. (1971), 121, 7.

Sign in / Sign up

Export Citation Format

Share Document