Partial purification and characterization of cysteine proteinase from metamorphosing tadpole tails of Rana catesbeiana |
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| Affiliation: | 1. Grupo de Investigación en Biología Evolutiva (GIBE), IEGEBA (CONICET–UBA), FCEyN, — Pabellón II — 4to Piso. Labs 43–46. Cdad. Universitaria, Intendente Güiraldes 2160, CP: 1428EGA Buenos Aires, Argentina;2. Laboratorio de Zoología Aplicada: Anexo Vertebrados (FHUC, UNL/MASPyMA), Aristóbulo del Valle 8700, CP: 3000, Santa Fe, Argentina;3. Instituto de Ciencias Veterinarias del Litoral (ICiVet-CONICET), R.P. Kreder 2805, CP: S3080HOF Esperanza, Santa Fe, Argentina;4. Cátedra de Toxicología, Farmacología y Bioquímica Legal (FBCB, UNL), Ciudad Universitaria Paraje El Pozo, CP: 3000, Santa Fe, Argentina;1. Graduate Program in Animal Biology, Department of Chemistry and Environmental Sciences, Universidade Estadual Paulista “Júlio de Mesquita Filho”, Cristóvão Colombo, 2265, 15054-000 São José do Rio Preto, SP, Brazil;2. Universidade Estadual de Goiás, Campus de Ciências Exatas e Tecnológicas, BR 153 n° 3105 - Fazenda Barreiro do Meio, CEP: 75132-903 Anápolis, GO, Brazil;3. Department of Natural Sciences, Fundação Universidade Regional de Blumenau, Av. Antonio da Veiga 140, Itoupava Seca, 89030-903 Blumenau, Santa Catarina, Brazil |
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| Abstract: | - 1.1. A leupeptin-sensitive proteinase was partially purified from regressing tadpole tails by acetone factionation and column chromatography on S-Sepharose.
- 2.2. The enzyme degraded hemoglobin and myoglobin at pH 3.0. The enzyme also hydrolyzed Z-Phe-Arg-MCA and Boc-Val-Leu-Lys-MCA at pH 4.0.
- 3.3. The enzyme activity was inhibited by leupeptin, egg cystatin, E-64 and monoiodoacetic acid and was activated by l-cysteine.
- 4.4. The enzyme degraded myosin and actin in myofibrils of tadpole tails.
- 5.5. The enzyme belongs to the cysteine proteinase and is possibly involved in tail degradation during the metamorphosis of tadpoles.
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