Biopolym. Cell. 1998; 14(3):196-202.
http://dx.doi.org/10.7124/bc.0004CE
Structure and Function of Biopolymers
Investigation of the primary structure of Penicillium vitale catalase. 4. Cyanogen bromide fragments
1Bobrovskaya M. T., 1Rodnin N. V., 1Levitina T. L., 2Latyshko N. V., 2Gudkova L. V., 1Kozlov E. A.
  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

The amino acid sequence of 9 Penicillium vitale catalase cyanogen bromide fragments was studied. These fragments comprise 477 amino acid residues what makes up 68 % of the catalase poly-peptide chain.
Full text: (PDF, in Russian)

References

[1] Levitina TL, Gusak NM, Rodnin NV, Kirilenko MT, Miroshnichenko OS, Atepalikhina SA, Gudkova LV, Kozlov EA. Cyanogen bromide fragments of Penicillium vitale catalase. Biopolym Cell. 1989; 5(5):55-63.
[2] Kozlov EA, Levitina TL, Bobrovskaya MT, Rodnin NV, Miroshnichenko OS, Latischko NV, Gudkova LV. Additional investigation of Penicillium vitale catalase cyanogen bromide fragments. Biopolym Cell. 1994; 10(2):45-8.
[3] Gusak NM, Levitina TL, Bobrovskaya MT, Gudkova LV, Kozlov EA. Investigation of the primary structure of Penicillium vitale catalase. 1. Tryptic peptides of nonmodified catalase. Biopolym Cell. 1998; 14(1):62-7.
[4] Levitina TL, Gusak NM, Miroshnichenko OS, Sobrovskaya MT, Gudkova LV, Latyshko NV, Kozlov EA. Investigation of the primary structure of Penicillium vitale catalase. 2. Tryptic peptides of maleilated catalase. Biopolym Cell. 1998; 14(2):105-10.
[5] Levitina TL, Latyshko NV, Bobrovskaya MT, Gudkova LV, Kozlov EA. Investigation of the primary structure of Penicillium vitale catalase. 3. Peptides obtained by cleavage of the catalase by Staphylococcus aureus V8 proteinase. Biopolym Cell. 1998; 14(3):191-5.