Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/100219
Type: Artigo de periódico
Title: Bovine Kidney Low Molecular Weight Acid Phosphatase: Fmn-dependent Kinetics
Author: Granjeiro J.M.
Ferreira C.V.
Juca M.B.
Taga E.M.
Aoyama H.
Abstract: A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p-nitrophenyl phosphate- (45.44 kJ mol-1) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2 and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction.
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Rights: fechado
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Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030976268&partnerID=40&md5=ac36a6aab0f568548dbc4296b2ce9ee8
Date Issue: 1997
Appears in Collections:Unicamp - Artigos e Outros Documentos

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