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Indian J Biochem Biophys ; 1990 Apr; 27(2): 93-7
Artigo em Inglês | IMSEAR | ID: sea-26340

RESUMO

A detergent solubilised sucrase from monkey small intestine has been purified 388-fold to gel electrophoretic homogeneity with an overall recovery of 36%. The molecular weight of the enzyme was 263 kDa by gel filtration. Electrophoresis in the presence of SDS indicates that the enzyme is a hetero-dimer. Mixed substrate inhibition studies and inhibition by PCMB and Tris suggest the presence of two catalytically active sites in the form of maltase and sucrase with isomaltase activity being common to both sites. Polyclonal antiserum against the purified enzyme showed a single continuous precipitin line with the purified antigen.


Assuntos
Animais , Sítios de Ligação , Haplorrinos/metabolismo , Intestino Delgado/enzimologia , Sacarase/metabolismo
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