Changes in proteinase activities and subcellular distribution during inactivation of alcohol oxidase in Candida boidinii.

Hill, David J., Jenkins, Richard O., Cartledge, Trevor G. and Lloyd, David ORCID: https://orcid.org/0000-0002-5656-0571 1986. Changes in proteinase activities and subcellular distribution during inactivation of alcohol oxidase in Candida boidinii. The Biochemical Journal 238 (1) , pp. 255-261. 10.1042/bj2380255

Full text not available from this repository.

Abstract

Adaptation of methanol-grown Candida boidinii to ethanol utilization was accompanied by an increase in proteolytic activities, which behaved like known vacuolar enzymes. Degradation of alcohol oxidase protein was partially prevented by the serine proteinase inhibitor phenylmethanesulphonyl fluoride, but not by the carboxyl proteinase inhibitor pepstatin. Fractionation of cell-free extracts, by high-speed zonal centrifugation, of methanol-grown C. boidinii showed non-sedimentable and sedimentable proteolytic activities. Naturally occurring inhibitors of vacuolar proteinases were non-sedimentable. Fractionation of extracts prepared from methanol-grown cells which had been adapted to ethanol utilization for 5 h revealed significant changes in the sedimentability and distribution of proteolytic and acid phosphatase activities. These results suggest the possible involvement of a vacuolar process during alcohol oxidase degradation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
ISSN:	0264-6021
Last Modified:	26 Oct 2022 08:38
URI:	https://orca.cardiff.ac.uk/id/eprint/127952

Citation Data

Cited 2 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item