Serine proteinase from rice bean.
Indian J Biochem Biophys
;
1996 Dec; 33(6): 491-7
Artigo
em Inglês
| IMSEAR
| ID: sea-27013
ABSTRACT
A trypsin like serine-proteinase of M(r) 16,000 Da, optimally active at pH 8.4 on N-benzoyl-arginine ethyl ester (BAEE) was purified from 4-day old germinated seeds of rice bean, Vigna umbellata (Thunb), by ammonium sulphate precipitation, gel filtration, ion-exchange chromatography and by high performance liquid chromatography (HPLC). The purity of the enzyme was checked by polyacrylamide gel electrophoresis (PAGE). The enzyme activity was studied on natural substrates like casein, haemoglobin and vicilin, a rice bean storage protein. The activity of the enzyme was completely inhibited by phenylmethylsulfonyl fluoride, but not by iodoacetamide and HgCl2, suggesting it to be a serine protease. Loss of activity in presence of EDTA was reversed by addition of Ca2+.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Plantas Medicinais
/
Especificidade por Substrato
/
Temperatura
/
Serina Endopeptidases
/
Cinética
/
Cálcio
/
Cromatografia Líquida de Alta Pressão
/
Cromatografia por Troca Iônica
/
Ácido Edético
/
Eletroforese em Gel de Poliacrilamida
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
1996
Tipo de documento:
Artigo
Similares
MEDLINE
...
LILACS
LIS