THE PRIMARY STRUCTURE OF THE CYTOCHROME c FROM VARIOUS ORGANS OF THE HOG

1965 ◽  
Vol 43 (7) ◽  
pp. 1187-1206 ◽  
Author(s):  
J. W. Stewart ◽  
E. Margoliash
Keyword(s):  
Cytochrome C ◽  
Polypeptide Chain ◽  
The Body ◽  
Horse Heart Cytochrome ◽  
Functional Activities ◽  
Amino Terminal ◽  
Single Polypeptide Chain ◽  
Molecular Variants ◽  
Single Polypeptide ◽  
Horse Heart Cytochrome C

The amino acid sequence of hog heart cytochrome c was determined. Like the horse and human heart proteins it was found to consist of a single polypeptide chain 104 residues long with a N-acetylated amino-terminal residue. It differs from horse heart cytochrome c in only three positions, carrying serine instead of threonine at residue 47, glycine instead of lysine at residue 60, and glycine instead of threonine at residue 89. Methods are described for the preparation of cytochrome c, in good yield, from hog liver, kidney, brain, and skeletal muscle. These proteins were all shown to have primary structures identical with that of hog heart cytochrome c, indicating that, notwithstanding differences in the functional activities and embryological origins of the various tissues examined, there is no corresponding change in the structure of cytochrome c. It thus appears likely that the synthesis of all, or at least the bulk, of the cytochrome c is controlled by a single structural gene throughout the body. Minor molecular variants of the protein, which could have been detected at concentrations of 2 to 3% of the entire preparations, were not observed.

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 primary structure of cytochrome c from the rust fungus Ustilago sphaerogena

1972 ◽  
Vol 129 (3) ◽  
pp. 561-569 ◽  
Author(s):  
K. G. Bitar ◽  
S. N. Vinogradov ◽  
C. Nolan ◽  
L. J. Weiss ◽  
E. Margoliash
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Primary Structure ◽  
Polypeptide Chain ◽  
Rust Fungus ◽  
Single Polypeptide Chain ◽  
C Terminus ◽  
Cytochromes C ◽  
Single Polypeptide ◽  
Asparagine Residue

1. The complete amino acid sequence of cytochrome c from the basidiomycete Ustilago sphaerogena was determined from the amino acid compositions and sequences of either tryptic or chymotryptic peptides, and in homology with at least thirty other established sequences of cytochrome c. 2. The primary structure of the molecule bears all of the characteristics of a mammalian-type cytochrome c, showing the typical clustered distribution of hydrophobic and basic residues with a single polypeptide chain of 107 residues. 3. Like all other fungal cytochromes c, it possesses a free N-terminus, and one less residue at the C-terminus than vertebrate cytochromes c. The region of residues 70–80 is strictly conserved, as is histidine at position 18. Position 26 is occupied by an asparagine residue, in contrast to histidine which occurs at this location in most of the known sequences of mammalian-type cytochromes c. 4. In contrast to some other fungal and plant cytochromes c of known primary structures, the Ustilago cytochrome c molecule does not contain trimethyl-lysine. 5. The sequence of Ustilago cytochrome c differs from the sequences of human, horse, chicken, tuna, wheat, and baker's yeast proteins at loci 47, 43, 44, 44 and 38 respectively.

scholarly journals Amino acid sequences of cytochrome c-554(548) and cytochrome c' from a halophilic denitrifying bacterium of the genus Paracoccus

1987 ◽  
Vol 248 (2) ◽  
pp. 365-371 ◽  
Author(s):  
R P Ambler ◽  
M Daniel ◽  
L McLellan ◽  
T E Meyer ◽  
M A Cusanovich ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Polypeptide Chain ◽  
Amino Acid Sequences ◽  
Desulfovibrio Vulgaris ◽  
Single Polypeptide Chain ◽  
Similar Protein ◽  
Cytochromes C ◽  
Single Polypeptide ◽  
Thiobacillus Neapolitanus

The amino acid sequences of the cytochromes c-554(548) and c' from the moderately halophilic bacterium Paracoccus sp., I.A.M. 203 (= A.T.C.C. 12084, N.C.I.B. 8669) have been determined. Cytochrome c-554(548) consists of a single polypeptide chain of 83 residues, and dimerizes strongly. The most similar protein of known sequence is the N-terminal half of the dihaem cytochrome c4, and other related proteins include the cytochrome c-554(547) of Thiobacillus neapolitanus and the cytochrome c-553 of Desulfovibrio vulgaris. Cytochrome c', which has a single polypeptide chain of 132 residues, is similar in sequence to cytochromes c' from phototrophic and denitrifying bacteria, but only shows about 36% sequence identity to the most similar protein of known sequence. Both of the Paracoccus proteins have a considerable excess of acidic amino acid side chains over basic ones, and a higher proportion of their basic amino acids is arginine than is usual in cytochromes c. Both these characteristics seem to be adaptations to increase the stability of the proteins in an environment of high ionic strength. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication 50140 (24 pp.) at the British Library (Lending Division), Boston Spa, Yorkshire LS23 7BQ, U.K. from which 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.

Kinetics and mechanism of the reaction between oxidized cytochrome c and ascorbic acid

1991 ◽  
Vol 56 (2) ◽  
pp. 478-490 ◽  
Author(s):  
Joaquin F. Perez-Benito ◽  
Conchita Arias
Keyword(s):  
Ascorbic Acid ◽  
Cytochrome C ◽  
Redox Reactions ◽  
Arrhenius Equation ◽  
Horse Heart Cytochrome ◽  
First Order ◽  
Acidic Form ◽  
Ph Range ◽  
Horse Heart Cytochrome C ◽  
Mechanism Of The Reaction

The reaction between horse-heart cytochrome c and ascorbic acid has been investigated in the pH range 5.5 – 7.1 and at 10.0 – 25.0 °C. The rate shows a first-order dependence on the concentration of cytochrome c, it increases in a non-linear way as the concentration of ascorbic acid increases, it increases markedly with increasing pH and, provided that the ionic strength of the medium is high enough, it fulfills the Arrhenius equation. The apparent activation energy increases as the pH of the solution increases. The results have been explained by means of a mechanism that includes the existence of an equilibrium between two forms (acidic and basic) of oxidized cytochrome c: cyt-H+ -Fe3+ + OH- cyt -Fe3+ + H2O, whose equilibrium constant is (6.7 ± 1.4). 108 at 25.0 °C, the acidic form being more reducible than the basic one. It is suggested that there is a linkage of hydrogenascorbate ion to both forms of cytochrome c previous to the redox reactions. Two possibilities for the oxidant-reductant linkage (binding and adsorption) are discussed in detail.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres
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