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L Gürtler1, H J. Horstmann

  • 1Institut für Physiologische Chemie, Wasserturmstr. 5,852, Erlangen, Germany

FEBS Letters
|October 15, 1971
PubMed
Summary
This summary is machine-generated.

Zebra cytochrome c differs from horse cytochrome c by one serine and nine threonine residues. These amino acid changes were identified at position 47 in the protein sequence.

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Area of Science:

  • Biochemistry
  • Comparative genomics
  • Protein analysis

Background:

  • Cytochrome c is a crucial protein in cellular respiration.
  • Variations in cytochrome c sequences can provide insights into evolutionary relationships.
  • Understanding protein structure differences is key to functional analysis.

Purpose of the Study:

  • To identify and characterize the specific amino acid differences between zebra (Equus guagga Boehmi) and horse cytochrome c.
  • To pinpoint the location of these sequence variations within the cytochrome c polypeptide chain.

Main Methods:

  • Amino acid sequencing of zebra cytochrome c.
  • Comparison of the zebra cytochrome c sequence with known horse cytochrome c sequences.
  • Sequence alignment to identify specific residue differences and their positions.

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Main Results:

  • Zebra cytochrome c contains one serine residue, whereas horse cytochrome c has none.
  • Zebra cytochrome c has nine threonine residues, differing from the ten found in horse cytochrome c.
  • These amino acid substitutions are localized to position 47 of the protein sequence.

Conclusions:

  • Zebra and horse cytochrome c exhibit distinct amino acid compositions.
  • The identified differences at position 47 highlight specific evolutionary divergence points.
  • Further studies can explore the functional implications of these structural variations.