Chemical denaturation studies of two isozymes of aryl-B-glucosidasein neurospora

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Susan Rawles Morton (Creator)
The University of North Carolina at Greensboro (UNCG )
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Bruce Eberhart

Abstract: The effect of guanidine hydrochloride (GuHCl) on the stability and the state of aggregation of Neurospora aryl-B-glucosldase isozymes "Y" and "W" was studied in one wild type and several exotic strains by two major methods. Purified conidial "Y" enzyme was treated with GuHCl and separated by electrophoresis on cellulose polyacetate and thin-layer gel (TLG) filtration on Biogel P-150. The inactivation characteristics in time of crude conidial washes and purified "Y" and "W" preparations were determined using p-nitrophenyl-S-D-glucopyranoside as the substrate. The generation of the smaller isozyme "W" from purified conidial "Y" was observed in the exotic strain P-212 with various concentrations (2 to 5M) of GuHCl, but not in the wild type strain STA-4 with 3M GuHCl. When P-212 "Y" was incubated with GuHCl at 4 C or at room temperature in the presence of 0.005M 2-mercaptoethanol, a new enzymatically active intermediate with a mobility on TLG between that of "Y" and "W" was observed.

Additional Information

Language: English
Date: 1975
Neurospora crassa

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