Biopolym. Cell. 1996; 12(5):46-49.
The amino acid sequence around the cystein residue of Penicillium vitale catalase
1Miroshnitchenko O. S., 1Levitina T. L., 1Bobrovskaya M. T., 1Kozlov E. A.
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
Abstract
The P. vitale catalase polypeptide chain was shown to contain 1 residue of cystein. 5 peptides from the polypeptide chain region containing the cystein residue were obtained and their structure was elucidated. The amino acid sequence around the cystein residue, including 31 amino acid residues, was reconstructed.
Full text: (PDF, in Russian)
References
[1]
Gudkova LV, Kirilenko MT, Levitina TL, Kozlov EA. Study of the subunit structure of catalase from Penicillium vitale. Ukr Biokhim Zh. 1985;57(4):29-33.
[2]
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.
[3]
Kozlov EA, Gudkova LV, Levitina TL, Kirilenko MT, Miroshnichenko OS. Additional investigation of Penicillium vitale catalase tryptic peptides. Biopolym Cell. 1993; 9(1):22-5.
[4]
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.
[5]
Levitina TL, Bobrovskaja MT, Gusak NM, Miroschnichenko OS, Gudkova LV, Latyschko NV, Kozlov EA. Tryptic peptides of Penicillium vitale maleyl-catalase. 2. The structure peptides. Biopolym Cell. 1993; 9(3):42-5.
[6]
Bobrovskaya MT, Latischko NV, Levitina TL, Miroschnichenko OS, Gudkova LV, Kozlov EA. The structure of some peptides obtained by means of cleavage of Penicillium vitale catalase by Staphylococcus proteinase. Biopolym Cell. 1994; 10(2):49-51.
[7]
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.
[8]
Egorov TsA, Shakhparonov MI, Davidovitch YuA, Losinsky VI, Zaslavsky BYu, Rogozhin SV. The preparation of insoluble support with activated SH-groups and its use in protein chemistry. Russian Journal of Bioorganic Chemistry 1977; 3 (8):1111-6
[9]
Ovchinnikov YUA, Abdulova NG, Bogachuk AS. Using covalent chromatography to study the structure of membrane proteins. Biol membrany. 1985; 2(10):962-75.
[10]
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.
[11]
Hirs CHW. Determination of cystine as cysteic acid. Methods Enzymol. 1967;59–62.
[12]
Easley CW. Combinations of specific color reactions useful in the peptide mapping technique. Biochim Biophys Acta. 1965;107(2):386–8.
[13]
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.
