THE PRIMARY STRUCTURE OF THE α POLYPEPTIDE CHAIN OF A11 COMPONENT OF ADULT CHICKEN HEMOGLOBIN

2009 ◽  
Vol 3 (1-4) ◽  
pp. 173-174 ◽  
Author(s):  
Genji Matsuda ◽  
Hiroshi Takei Ku Chayu Wu ◽  
Tsuneo Shiozawa
Keyword(s):  
Primary Structure ◽  
Polypeptide Chain ◽  
Adult Chicken

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 Preliminary results for the primary structure of bacterioferritin of Escherichia coli

1985 ◽  
Vol 231 (1) ◽  
pp. 209-212 ◽  
Author(s):  
A Tsugita ◽  
J Yariv
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Chemical Modification ◽  
Primary Structure ◽  
Amino Acid Analysis ◽  
Polypeptide Chain ◽  
Type B ◽  
Methionine Residue ◽  
Methionine Residues

Bacterioferritins are type-b cytochromes which resemble ferritin. Amino acid analysis combined with chemical modification and partial sequence analysis characterize bacterioferritin of Escherichia coli in terms of its primary structure. It is a protein composed of one kind of polypeptide chain that commences with methionine and terminates with glutamic acid. The length of the polypeptide chain is, tentatively, 146 residues. Besides the N-terminal methionine residue there are three more methionine residues, which yield four CNBr peptides, which have been aligned. The identity of the following positions in the sequence has been ascertained: residues 1-25, 30-37, 83-88, 127-132 and 143-146. No homology with ferritin was found.

THE PRIMARY STRUCTURE OF THE β POLYPEPTIDE CHAIN OF ADULT HEMOGLOBIN OF THE JAPANESE MONKEY (Macaca fuscata fuscata)

2009 ◽  
Vol 3 (1-4) ◽  
pp. 53-55 ◽  
Author(s):  
Genji Matsuda ◽  
Tetsuo Maita ◽  
Hisahiro Ota ◽  
Isamu Tachikawa ◽  
Yoshiro Tanaka ◽  
...  
Keyword(s):  
Primary Structure ◽  
Macaca Fuscata ◽  
Polypeptide Chain ◽  
Japanese Monkey ◽  
Macaca Fuscata Fuscata ◽  
Adult Hemoglobin
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