Investigation of the Active Center of Porcine‐Pancreatic Amylase

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dc.contributor.authorElödi P.
dc.contributor.authorMóra S.
dc.contributor.authorKrysteva M.
dc.date.accessioned2024-07-10T14:27:02Z
dc.date.accessioned2024-07-10T14:46:52Z
dc.date.available2024-07-10T14:27:02Z
dc.date.available2024-07-10T14:46:52Z
dc.date.issued1972-01-01
dc.description.abstractThe effect of maltose was studied in porcine pancreatic amylase. At neutral pH 1% (29 mM) maltose produced with amylase a difference spectrum characteristic of the perturbation of tryptophan. The molar absorption difference at the maximum wavelength was Δ290= 1200. The difference spectrum appeared to be specific for maltose. Perturbation difference spectra measurements in 20% polyethylene glycol indicated that one tryptophyl side chain per mol amylase was involved in the interaction with maltose. The dissociation constant of the amylase · maltose complex calculated from the concentration dependence of the absorption difference at 290 nm was Ks= 13 mM. Maltose inhibited amylase activity competitively and an inhibition constant of Ki= 25 mM was obtained, a similar value to that found spectrophotometrically. It is assumed that the tryptophyl side chain interacting with maltose may be involved in the binding of substrate by pancreatic amylase. Copyright © 1972, Wiley Blackwell. All rights reserved
dc.identifier.doi10.1111/j.1432-1033.1972.tb19720.x
dc.identifier.issn1432-1033
dc.identifier.issn0014-2956
dc.identifier.scopusSCOPUS_ID:0015518062en
dc.identifier.urihttps://rlib.uctm.edu/handle/123456789/45
dc.language.isoen
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0015518062&origin=inward
dc.titleInvestigation of the Active Center of Porcine‐Pancreatic Amylase
dc.typeArticle
oaire.citation.issue3
oaire.citation.volume24
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