Biopolym. Cell. 2001; 17(4):283-291.
Structure and Function of Biopolymers
Revision of tryptic peptides and cyanogen bromide fragments structure of Penicillium vitale catalase
1Kozlov E. A., 1Levitina T. L., 1Bobrovskaja M. T., 1Ovander M. N., 1Gudkova L. V., 1Latyshko N. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Revision of ammo acid sequence of unmodified and maleilate Penicillium vitale catalase tryptic and cyanogen bromide peptides was made.

References

[1] Kozlov EA, Levitina TL, Bobrovskaia MT, Gudkova LV, Latyshko NV, RadomskiД­ NF. Complete amino acid sequence of catalase from the fungus Penicillium vitale. Bioorg Khim. 1998;24(3):163-70.
[2] Kozlov EA, Levitina TL, Bobrovskaya MT, Gudkova LV, Radomskij NF. Investigation of the Penicillium vitale catalase primar structure. 5. Reconstruction of the polypsptide chain and comparison it with other catalases. Biopolym Cell. 1998; 14(4):320-331.
[3] 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.
[4] 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.
[5] 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.
[6] 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.
[7] Kirilenko MT, Levitina TL, Gudkova LV, Degtiar RG, Kozlov EA. Tryptic peptides of Penicillium vitale catalase. 2. Isolation and amino acid composition of unsoluble peptides. Biopolym Cell. 1988; 4(1):40-3.
[8] Levitina TL, Miroschnichenko OS, Gudkova LV, Bobrovskaya MT, Latyschko NV, Kozlov EA. Tryptic peptides of Penicillium vitale maleyl-catalase. 1. Isolation and amino acid composition. Biopolym Cell. 1993; 9(2):3-8.
[9] 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.
[10] Palchikovskaya LI, Levitina TL, Bobrovskaya MT, Ovander MN, Katsman MS, Kozlov EA. Accelerated method of determination of the high-homologous proteins primary structures. Complete amino acid sequence of Mamestra brassicae nuclear polyhedrosis virus (NPV) polyhedrin. Biopolym Cell. 1993; 9(4):44-9.
[11] Gusak NM, Ovander MN, Drobot LB, Serebryanyy SB. Determining the structure of peptides combined method Dansyl-Edman. Molecular methods. biology. Kiev, Naukova Dumka, 1979; 142-54.
[12] Miroshnitchenko OS, Levitina TL, Bobrovskaya MT, Kozlov EA. The amino acid sequence around the cystein residue of Penicillium vitale catalase. Biopolym Cell. 1996; 12(5):46-9.
[13] Bobrovskaya MT, Rodnin NV, Levitina TL, Latyshko NV, Gudkova LV, Kozlov EA. Investigation of the primary structure of Penicillium vitale catalase. 4. Cyanogen bromide fragments. Biopolym Cell. 1998; 14(3):196-202.
[14] 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.