Biopolym. Cell. 1993; 9(1):22-25.
Structure and Function of Biopolymers
Additional investigation of Penicillium vitale catalase tryptic peptides
1Kozlov E. A., 2Gudkova L. V., 1Levitina T. L., 2Kirilenko M. T., 1Miroshnichenko O. S.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601

Abstract

26 peptides containing 364 amino acid residues were isolated from tryptic hydrolizate of the Penicillium vitale catalase. Partial or complete amino acid sequence of these peptides was determined. The total number of peptides described herein as well as those published previously is 68.65 peptides have non-overlapping sequences comparising 595 amino acid residues (86 % of catalase polypeptide chain).

References

[1] Kozlov EA, Kirilenko MT, Levltina TL, Gudkova LV, Degtyar RG, Solodova EV. Tryptic peptides of Penicillium vitale catalase. 1. Isolation and amino acid composition of soluble peptides. Biopolym Cell. 1987; 3(5):240-5.
[2] Kozlov EA, Levitina TL, Gusak NM, Rodnin NV, Gudkova LV, Kirilenko MT, Degtyar RG. Polypeptide chain fragments of the Penicillium vitale catalase. Biopolym Cell. 1987; 3(6):318-20.
[3] Gusak NM, Levitina TL, Atepalikhina SA, Kirilenko MT, Gudkova LV, Kozlov EA Tryptic peptides of Penicillium vitale catalase. 3. The structure of some peptides. Biopolym Cell. 1989; 5(1):45-51.
[4] Vainshtein BK, Melik-Adamyan WR, Barynin VV, Vagin AA, Grebenko AI, Borisov VV, Bartels KS, Fita I, Rossmann MG. Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution. J Mol Biol. 1986;188(1):49-61.