Revista de Biología Tropical ISSN Impreso: 0034-7744 ISSN electrónico: 2215-2075

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Estudio comparativo de las isoenzimas de L-aminoácido oxidasa del veneno de <i>Bothrops asper</i>
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Umaña, V. (1982). Estudio comparativo de las isoenzimas de L-aminoácido oxidasa del veneno de <i>Bothrops asper</i>. Revista De Biología Tropical, 30(1), 79–84. Retrieved from https://revistas.ucr.ac.cr/index.php/rbt/article/view/25347

Abstract

A comparative study was performed between the isozymes 1 and 2b of the L-amino acid oxidase (E.C.1.4.3.2) from the venom of Bothrops asper snakes captured in Costa Rica. The amino acid composition differs slightly: L-amino acid oxidase-1 (thn most anodal) shows more aspartic and glutamic acid residues than L-amino acid oxidase-2b, which was found to be richer in lysine and alanine residues. Both isozymes had subunits of 60.000 and 57,000 molecular weight, as shown by electrophoresis on SDS polyacrylamide gel. Results of peptide mapping studies are consistent with a high degree of homology between the compared isozymes, and the number of peptides obtained indicated homologous subunits.
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References

Bennett, J.C. 1967. Paper chromatography and electrophoresis. Special procedure for peptide maps, p. 330-339. In S.P. Colowick and N.O. Kaplan (eds.), Methods in Enzymology, Vol. XI. Academic Press. New York.

De Kok, A., & A.B. Rawitch. 1969. Studies on L-amino acid oxidase. II. Dissociation and characterization of its subunits. Biochemistry, 8: 1405-1411.

Ounker, A.K. & R.R. Rueckert. 1969. Observations on molecular weight determinations on polyacrilamide gel. J. Biol. Chem. 244: 5074-5080.

Easley, C.W. 1965. Combinations of specific color reactions useful in the peptide mapping technique. Biocrum. Biophys. Acta, 107: 386-388.

Koska, V. & F.H. Carpenter. 1964. Inhibition of chyrnotrypsin activity in crystalline trypsin preparations. J. Biol. Chem., 239: 1799-1803.

Lindly, H.A. 1956. A new synthetic substrate for trypsin and its application to the determination of the amino acid sequence of proteins. Nature, 178: 647-648.

Maizel. J.V. 1966. Acrylamide gel electrophorograms by mechanical fractionation: radioactive adenovirus proteins. Science, 151: 988-990.

Moore, S., & W.H. Stein. 1963. Chromatographic determination of amino acids by the use of automatic recording equiprnent, p. 819-831. In S.P. Colowick and N.O. Kaplan (eds.), Methods in Enzyrnology, Vol. VI. Academic Press. New York.

Putnam, F.W. & C.W. Basley. 1965. Structural studies of the immunoglobulins. I. The tryptic peptides of Bence-Jones proteins. J . Biol. Chem., 240: 1626-1638.

Raftery, M.A. & R.O. Coleo 1963. Tryptic cleavage at cysteinyl peptide bonds. Biochim. Biophys. Res. Comm., 10: 467-472.

Raftery, M.A., & R.O. Cole. 1966. On the amino ethylation of proteins. J. Biol. Chern., 241: 3457-3461.

Shapiro, A.L., E. Vinuela & J.V. Maizel. 1967. Molecular weight estimation of polypeptide chains by electrophoresis in SOS-polyacrylamide gels. Biochim. Biophys. Res. Comm., 28: 815-820.

Smyth, D.G. 1967. Techniques in enzyrnic hydrolysis, p. 214-231. In S.P. Colowick and N.O. Kaplan (eds.). Methods in Enzyrnology. Vol. XI. Academic Press. New York.

Spackman, O.H., W.H. Stein & S. Moore. 1958. Automatic recording apparatus for use in the chroma tography of amino acids. Anal. Chem., 30: 1190-1206.

Spies, J.R. & D.C. Chambers. 1949. Chemical determination of tryptophan in proteins. Anal. Chem., 21: 1249-1266.

Umaña, V. 1982. Purificación y separación de isoenzimas de L-aminoácido oxidasa del veneno de Bothrops asper. Rev. Biol. Trop., 30: 59-64.

Wellner, D. & A. Meister. 1960. Crystalline L-amino acid oxidase of Crotalus adamanteus. J. Biol. Chem., 235: 2013-2018.

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