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J. Biochem, 1968, Vol. 63, No. 2 226-241
© 1968 Japanese Biochemical Society

research-article

The Amino Acid Sequence of Cytochrome c from Candida krusei

KOZO NARITA and KOITI TITANI

From the Institute for Protein Resarch, Osaka University Kita-ku, Osaka

Twenty-one peptides were isolated from the tryptic digest of Candida krusei cytochrome c by chromatography on columns of Amberlite CG-50 and Dowex 50-X2. The amino acid sequence in these peptides was determined solely by the use of several non-enzymatic methods without the use of proteolytic enzymes. The arrangement of the twenty-one peptides into a linear structure could easily be made by referring to the primary structure of Saccharomyces oviformis cutochrome c which had previously been elucidated. The following 109 amino acid residues were concluded to be present in one molecule of Candida cytochrome c, on the basis of the completed primary structure (Scheme 1):

Lys12, His4, Arg4, Trp1, Asp4, AsN4, Thr7, Ser6, Glu8, GlN2, Pro7,

Gly12, Ala12, Cys2, Val2, Met3, Ile3, Leu6, Tyr5, and Phe4.


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