Substrate specificity of methylthioadenosine phosphorylase from human liver

• Autorzy: Fabianowska-Majewska K. , Duley J. , Fairbanks L. , Simmonds A. , Wasiak T.
• Języki publikacji: EN

Abstrakty

Methylthioadenosine (MTA) phosphorylase purified 615-fold from human liver cleaved phosphorolytically nucleoside analogues at the decreasing specific activity: 5'-deoxyadenosine > 5'-iodo-5'-deoxyadenosine > MTA > adenosine > 2-chloro- adenosine > 2-chloro-5'-0-methyl-2'-deoxyadenosine > 2-chloro-2'-deoxyadenosine > > 2'-deoxyadenosine. Adenosine and analogues of 5'-deoxyadenosine were strong competitive inhibitors of MTA phosphorolysis catalysed by the human liver enzyme.

Słowa kluczowe

EN

methylthioadenosine phosphorylase; 2-chloroadenisine; man; 2'-deoxyadenosine; 2-chloro-2'-deoxyadenosine; liver

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1994
• Tom: 41
• Numer: 4
• Opis fizyczny: p.391-395

Twórcy

autor

Fabianowska-Majewska K.

• Medical University of Lodz, Lindleya 6, 90-131 Lodz, Poland

autor

Duley J.

autor

Fairbanks L.

autor

Simmonds A.

autor

Wasiak T.

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