Pregled bibliografske jedinice broj: 982094
Selective inhibition of alkaline phosphatases: limited access of the Escherichia coli active site to dialkyl substituted phenyl phosphates
Selective inhibition of alkaline phosphatases: limited access of the Escherichia coli active site to dialkyl substituted phenyl phosphates // Acta pharmaceutica, 42 (1992), 3; 203-209 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 982094 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Selective inhibition of alkaline phosphatases: limited access of the Escherichia coli active site to dialkyl substituted phenyl phosphates
(SELECTIVE-INHIBITION OF ALKALINE-PHOSPHATASES - LIMITED ACCESS OF THE ESCHERICHIA-COLI ACTIVE- SITE TO DIALKYL SUBSTITUTED PHENYL PHOSPHATES)
Autori
M PAVELA-VRANČIĆ, S ORHANOVIĆ, Mirna Flögel
Izvornik
Acta pharmaceutica (1330-0075) 42
(1992), 3;
203-209
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Isoenzymes ; Liver, CDNA ; Bone
Sažetak
The structural interrelationship and catalytic specifities of E. coli, calf intestinal and human alkaline phosphatases were investigated. The inhibition studies were performed using a variety of structural related alternative substrates i.e. dialkyl substituted phenyl phosphates. The absence of a major steric effect for disubstituted aryl monophosphates indicates considerable freedom of the leaving group in the ES complex of human ALPs. Calf intestinal and E. coli ALP behave in a similar manner being much less affected by the different inhibitors. The steric specifity of E. coli ALP is evidenced by the findings that bulky ortho-substituents on the aryl function reduce the inhibitory response of the respective alternative substrates.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Farmacija
POVEZANOST RADA
Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb,
Prirodoslovno-matematički fakultet, Split
Citiraj ovu publikaciju:
Časopis indeksira:
- Scopus