Research orientations in nursing--XX. Help! Where's the programme? The use of hand calculators and computer services.
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Biomedical subjects
Publications and source records attributed to A Bhaduri.
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UDPglucose-4-epimerase (EC 5.1.3.2) from Saccharomyces fragilis is inactivated by 0.1 mM 5,5'-dithiobis-(2-nitrobenzoate) in 6 min. Unlike p-chloromercuribenzoate-inactivated or heat-inactivated enzymes, the dithiobisnitrobenzoate-inactivated enzyme retains the dimeric structure and NAD is not dissociated from the protein moiety. Inactivation of the enzyme by dithiobisnitrobenzoate can not therefore be attributed to any subsequent loss of structural integrity or to the detachment of the cofactor from the apoenzyme. The inactivated enzyme can be almost fully reactivated in the presence of mercaptoethanol and characteristic properties of native enzyme are regained. The inactivation by dithiobisnitrobenzoate can be substantially protected by UDPglucose or UDPgalactose indicating a possible critical involvement of one or more sulfhydryl groups at the active site.
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UDP-glucose 4-epimerase from Saccharomyces fragilis is rapidly inactivated by heating at 42 degrees C for 7 min and at 45 degrees C for 4 min. The effector site, specific for sugar phosphates, is destroyed still earlier. The enzyme is inactivated by the dissocation of NAD from it leaving the dimeric structure unaffected. It can be reactivated by mercaptoethanol and NAD, both of which are essential for reactivation, and NAD becomes associated with the dimeric protein moiety.
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