Subunit structure and carbohydrate composition of the extracellular acid phosphatase of Rhodotorula glutinis.
Year: 1981
Type: article
Abstract: The extracellular acid phosphatase (EC 3.1.3.2) of Rhodotomla glutinis is a glycoenzyme composed of 6 0 8 protein, 35% mannose, and 5% N-acetylglucosamine by weight.The native enzyme elutes from a column of Bio-Gel A-5M agarose with an M, 5 185,000 but on sodium dodecyl sulfate-acrylamide gel electrophoresis migrates with an M, = 93,000.The acid phosphatase thus appears to consist of two subunits of equal size, a conclusion also supported by cross-linking experiments with dimethyl suberimidate.Digestion of denatured acid phosphatase with endo-8-N-acetylglucosaminidase H from Streptomyces plicatus removes 80% of the mannose and 50% of the N-acetylglucosamine, with the remaining mannose liberated either by a-mannosidase or by alkaline /3 elimination.The carbohydratedepleted protein has an Mr = 59,500 by sodium dodecyl sulfate-acrylamide gel electrophoresis and by ultracentrifugation in 6 M guanidine hydrochloride.The NH2 terminus appears to be blocked, as no amino acid residues are released on 10 cycles of automated Edman degradation.However, COOH-terminal sequencing with carboxypeptidases A, B, and Y releases, in order,
Source: Journal of Biological Chemistry
Authors: R.B. Trimble, F. Maley, W. Watorek
Institutions: New York State Department of Health, University of Wrocław
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1495904420