Polypeptide chain fragments of the Penicillium vitale catalase

Authors

  • E. A. Kozlov Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • T. L. Levitina Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • N. M. Gusak Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • N. V. Rodnin Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • L. V. Gudkova Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • M. T. Kirilenko Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author
  • R. G. Degtyar Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR Kiev, USSR Author

DOI:

https://doi.org/10.7124/bc.000204

Abstract

Amino acid composition, partial or complete amino acid sequence of the Penicillium vitale catalase polypeptide chain fragments were determined. 55 unique fragments comprise 468 amino acid residues, and count 72 % of the catalase polypeptide chain.

References

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.

Levitina TL, Serebryany SB, Rodnin NV, Kozlov EA. The structure of some tryptic peptides of the Agrotis segetum granulosis virus granulin. Biopolym Cell. 1986; 2(1):30-5.

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.

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Published

1987-11-20

Issue

Vol. 3 No. 6 (1987)

Section

Short Communications