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Determination of the Molecular Weight of α-Amylase, as the Enzyme-Inhibitor Complex, using Thin Layer Gel Filtration on Sephadex by J. Kamarýt; J. Zemek; L’. Kuniak is a Medicine article available to read on EtoBox.

What is Determination of the Molecular Weight of α-Amylase, as the Enzyme-Inhibitor Complex, using Thin Layer Gel Filtration on Sephadex about?

Thin layer gel filtration on Sephadex was perfbrmed äs a simple method for recognition of the small molecular weight differences of human -amylases from different sources. Activity was located with dry chromogenic Substrate, using a replica technique. Undesirable interaction between the gel matrix and Substrate binding sites on the enzyme, which causes an anomalous decrease in the migration rate of the enzyme protein, was suppressed by preincubation of the enzyme with appropriate inhibitor. Gradual masking of Substrate binding sites of the enzyme by increasing concentrations of amyläse inhibitor resulted in two distinct migration rates for the enzyme in thin layer gel filtration. This suggests the existence of two Substrate binding sites in the enzyme molecule. Together with thin layer gel affinity chromatography on a mixture of Sephadex and ConA-Sepharose, the method yielded useful data on the molecular weight of amyläse and its glycosylated forms and served äs a valuable tool for the differential diagnosis of macroamylasaemia. ## Bestimmung des Molekulargewichtes von ot-Amylase als EnzymJnhibitor-Komplex mit Dünnschichtgelfiltration an Sephadex Zusammenfassung: Die Dünnschichtgel

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Author

J. Kamarýt; J. Zemek; L’. Kuniak

Publisher

Walter de Gruyter GmbH

Published

1982

Language

EN

Field

Medicine (Health Sciences)